Can be marine bioactive peptides (MBAs) lead the future of foodomics for human health?

References

• Achour, A., A. Lachgar, A. Astgen, V. Chams, B. Bizzini, H. Tapiero, and D. Zagury. 1997. Potentialization of IL-2 effects on immune cells by oyster extract (JCOE) in normal and HIV-infected individuals. Biomedicine & Pharmacotherapy = Biomedecine & Pharmacotherapie 51 (10):427–9. doi: 10.1016/S0753-3322(97)82320-7.
   PubMed Web of Science ®Google Scholar
• Afifi, A. H., A. H. El-Desoky, H. Kato, R. E. Mangindaan, N. J. de Voogd, N. M. Ammar, M. S. Hifnawy, and S. Tsukamoto. 2016. Carteritins A and B, cyclic heptapeptides from the marine sponge Stylissa carteri. Tetrahedron Letters 57 (11):1285–8. doi: 10.1016/j.tetlet.2016.02.031.
   Web of Science ®Google Scholar
• Ahhmed, A. M., and M. Muguruma. 2010. A review of meat protein hydrolysates and hypertension. Meat Science 86 (1):110–8. doi: 10.1016/j.meatsci.2010.04.032.
   PubMed Web of Science ®Google Scholar
• Amagata, T., B. I. Morinaka, A. Amagata, K. Tenney, F. A. Valeriote, E. Lobkovsky, J. Clardy, and P. Crews. 2006. A chemical study of cyclic depsipeptides produced by a sponge-derived fungus. Journal of Natural Products 69 (11):1560–5. doi: 10.1021/np060178k.
   PubMed Web of Science ®Google Scholar
• Anand, T. P., C. Chellaram, G. Kuberan, and H. Archana. 2012. Bioactive peptides from marine sources-a review. Indian Journal of Innovations and Developments 1:61–4.
   Google Scholar
• Andavan, G. S. B., and R. Lemmens-Gruber. 2010. Cyclodepsipeptides from marine sponges: Natural agents for drug research. Marine Drugs 8 (3):810–34. doi: 10.3390/md8030810.
   PubMed Web of Science ®Google Scholar
• Andjelic, C. D., V. Planelles, and L. R. Barrows. 2008. Characterizing the anti-HIV activity of papuamide A. Marine Drugs 6 (4):528–49. doi: 10.3390/md20080027.
   PubMed Web of Science ®Google Scholar
• Aneiros, A., and A. Garateix. 2004. Bioactive peptides from marine sources: Pharmacological properties and isolation procedures. Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences 803 (1):41–53. doi: 10.1016/j.jchromb.2003.11.005.
   PubMed Web of Science ®Google Scholar
• Arumugam, V., M. Venkatesan, S. Ramachandran, and U. Sundaresan. 2018. Bioactive peptides from marine ascidians and future drug development–A Review. International Journal of Peptide Research and Therapeutics 24 (1):13–8. doi: 10.1007/s10989-017-9662-9.
   Web of Science ®Google Scholar
• Balunas, M. J., R. G. Linington, K. Tidgewell, A. M. Fenner, L.-D. Urena, G. D. Togna, D. E. Kyle, and W. H. Gerwick. 2010. Dragonamide E, a modified linear lipopeptide from Lyngbya majuscula with antileishmanial activity. Journal of Natural Products 73 (1):60–6. doi: 10.1021/np900622m.
   PubMed Web of Science ®Google Scholar
• Battison, A. L., R. Summerfield, and A. Patrzykat. 2008. Isolation and characterisation of two antimicrobial peptides from haemocytes of the American lobster Homarus americanus. Fish & Shellfish Immunology 25 (1–2):181–7. doi: 10.1016/j.fsi.2008.04.005.
   PubMed Web of Science ®Google Scholar
• Baudin, E., J. P. Droz, L. Paz-Ares, A. T. van Oosterom, M. Cullell-Young, and M. Schlumberger. 2010. Phase II study of plitidepsin 3-hour infusion every 2 weeks in patients with unresectable advanced medullary thyroid carcinoma. American Journal of Clinical Oncology 33 (1):83–8. doi: 10.1097/COC.0b013e31819fdf5e.
   PubMed Web of Science ®Google Scholar
• Belofsky, G. N., P. R. Jensen, and W. Fenical. 1999. Sansalvamide: A new cytotoxic cyclic depsipeptide produced by a marine fungus of the genus Fusarium. Tetrahedron Letters 40 (15):2913–6. doi: 10.1016/S0040-4039(99)00393-7.
   Web of Science ®Google Scholar
• Bendell, J., M. Saleh, A. A. N. Rose, P. M. Siegel, L. Hart, S. Sirpal, S. Jones, J. Green, E. Crowley, R. Simantov, et al. 2014. Phase I/II study of the antibody-drug conjugate glembatumumab vedotin in patients with locally advanced or metastatic breast cancer. Journal of Clinical Oncology: Official Journal of the American Society of Clinical Oncology 32 (32):3619–25. doi: 10.1200/JCO.2013.52.5683.
   PubMed Web of Science ®Google Scholar
• Bertram, A., and G. Pattenden. 2007. Marine metabolites: Metal binding and metal complexes of azole-based cyclic peptides of marine origin. Natural Product Reports 24 (1):18–30. doi: 10.1039/b612600f.
   PubMed Web of Science ®Google Scholar
• Bhaskar, N., T. Benila, C. Radha, and R. G. Lalitha. 2008. Optimization of enzymatic hydrolysis of visceral waste proteins of Catla (Catla catla) for preparing protein hydrolysate using a commercial protease. Bioresource Technology 99 (2):335–43. doi: 10.1016/j.biortech.2006.12.015.
   PubMed Web of Science ®Google Scholar
• Blunt, J. W., B. R. Copp, R. A. Keyzers, M. H. Munro, and M. R. Prinsep. 2013. Marine natural products. Natural Product Reports 30 (2):237–323. doi: 10.1039/c2np20112g.
   PubMed Web of Science ®Google Scholar
• Boot, C. M., K. Tenney, F. A. Valeriote, and P. Crews. 2006. Highly N-methylated linear peptides produced by an atypical sponge-derived Acremonium sp. Journal of Natural Products 69 (1):83–92. doi: 10.1021/np0503653.
   PubMed Web of Science ®Google Scholar
• Bougatef, A., N. Nedjar-Arroume, R. Ravallec-Plé, Y. Leroy, D. Guillochon, A. Barkia, and M. Nasri. 2008. Angiotensin I-converting enzyme (ACE) inhibitory activities of sardinelle (Sardinella aurita) by-products protein hydrolysates obtained by treatment with microbial and visceral fish serine proteases. Food Chemistry 111 (2):350–6. doi: 10.1016/j.foodchem.2008.03.074.
   PubMed Web of Science ®Google Scholar
• Braekman, J. C., D. Daloze, B. Moussiaux, and R. Riccio. 1987. Jaspamide from the marine sponge Jaspis johnstoni. Journal of Natural Products 50 (5):994–5. doi: 10.1021/np50053a048.
   Web of Science ®Google Scholar
• Broggini, M., S. V. Marchini, E. Galliera, P. Borsotti, G. Taraboletti, E. Erba, M. Sironi, J. Jimeno, G. T. Faircloth, R. Giavazzi, et al. 2003. Aplidine, a new anticancer agent of marine origin, inhibits vascular endothelial growth factor (VEGF) secretion and blocks VEGF-VEGFR-1 (flt-1) autocrine loop in human leukemia cells MOLT-4. Leukemia 17 (1):52–9. doi: 10.1038/sj.leu.2402788.
   PubMed Web of Science ®Google Scholar
• Brust, A., E. Palant, D. E. Croker, B. Colless, R. Drinkwater, B. Patterson, C. I. Schroeder, D. Wilson, C. K. Nielsen, M. T. Smith, et al. 2009. chi-Conopeptide pharmacophore development: toward a novel class of norepinephrine transporter inhibitor (Xen2174) for pain. Journal of Medicinal Chemistry 52 (22):6991–7002. doi: 10.1021/jm9003413.
   PubMed Web of Science ®Google Scholar
• Byun, H.-G., and S.-K. Kim. 2001. Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin. Process Biochemistry 36 (12):1155–62. doi: 10.1016/S0032-9592(00)00297-1.
   Web of Science ®Google Scholar
• Byun, H.-G., J. K. Lee, H. G. Park, J.-K. Jeon, and S.-K. Kim. 2009. Antioxidant peptides isolated from the marine rotifer, Brachionus rotundiformis. Process Biochemistry 44 (8):842–6. doi: 10.1016/j.procbio.2009.04.003.
   Web of Science ®Google Scholar
• Carroll, A. R., B. F. Bowden, J. C. Coll, D. C. Hockless, B. W. Skelton, and A. H. White. 1994. Studies of Australian ascidians. IV. Mollamide, a cytotoxic cyclic heptapeptide from the compound ascidian Didemnum molle. Australian Journal of Chemistry 47 (1):61–9. doi: 10.1071/CH9940061.
   Web of Science ®Google Scholar
• Carroll, A. R., Y. Feng, B. F. Bowden, and J. C. Coll. 1996. Studies of Australian ascidians. 5. Virenamides A − C, new cytotoxic linear peptides from the colonial didemnid ascidian Diplosoma virens. The Journal of Organic Chemistry 61 (12):4059–61. doi: 10.1021/jo951379o.
   PubMed Web of Science ®Google Scholar
• Centenaro, G. S., M. S. Centenaro, and C. P. Hernandez. 2011. Antioxidant activity of protein hydrolysates of fish and chicken bones. Journal of Food Science Techology 3: 280–288.
   Google Scholar
• Chan, W. R., W. F. Tinto, P. S. Manchand, and L. J. Todaro. 1987. Stereostructures of geodiamolides A and B, novel cyclodepsipeptides from the marine sponge Geodia sp. The Journal of Organic Chemistry 52 (14):3091–3. doi: 10.1021/jo00390a023.
   Web of Science ®Google Scholar
• Charoensiddhi, S., M. A. Conlon, C. M. M. Franco, and W. Zhang. 2017. The development of seaweed-derived bioactive compounds for use as prebiotics and nutraceuticals using enzyme technologies. Trends in Food Science & Technology 70:20–33. doi: 10.1016/j.tifs.2017.10.002.
   Web of Science ®Google Scholar
• Chen, Z., Y. Song, Y. Chen, H. Huang, W. Zhang, and J. Ju. 2012. Cyclic heptapeptides, cordyheptapeptides C-E, from the marine-derived fungus Acremonium persicinum SCSIO 115 and their cytotoxic activities. Journal of Natural Products 75 (6):1215–9. doi: 10.1021/np300152d.
   PubMed Web of Science ®Google Scholar
• Cheung, R. C. F., T. B. Ng, and J. H. Wong. 2015. Marine peptides: Bioactivities and applications. Marine Drugs 13 (7):4006–43. doi: 10.3390/md13074006.
   PubMed Web of Science ®Google Scholar
• Ciavatta, M. L., F. Lefranc, M. Carbone, E. Mollo, M. Gavagnin, T. Betancourt, R. Dasari, A. Kornienko, and R. Kiss. 2017. Marine mollusk-derived agents with antiproliferative activity as promising anticancer agents to overcome chemotherapy resistance. Medicinal Research Reviews 37 (4):702–801. doi: 10.1002/med.21423.
   PubMed Web of Science ®Google Scholar
• Cioca, D., and K. Kitano. 2002. Induction of apoptosis and CD10/neutral endopeptidase expression by jaspamide in HL-60 line cells. Cellular and Molecular Life Sciences: CMLS 59 (8):1377–87. doi: 10.1007/s00018-002-8515-6.
   PubMed Web of Science ®Google Scholar
• Coleman, J. E., R. Van Soest, and R. J. Andersen. 1999. New geodiamolides from the sponge Cymbastela sp. collected in Papua New Guinea. Journal of Natural Products 62 (8):1137–41. doi: 10.1021/np990155o.
   PubMed Web of Science ®Google Scholar
• Costa, M., J. Costa-Rodrigues, M. H. Fernandes, P. Barros, V. Vasconcelos, and R. Martins. 2012. Marine cyanobacteria compounds with anticancer properties: A review on the implication of apoptosis. Marine Drugs 10 (10):2181–207. doi: 10.3390/md10102181.
   PubMed Web of Science ®Google Scholar
• Cude, W. N., J. Mooney, A. A. Tavanaei, M. K. Hadden, A. M. Frank, C. A. Gulvik, A. L. May, and A. Buchan. 2012. Production of the antimicrobial secondary metabolite indigoidine contributes to competitive surface colonization by the marine roseobacter Phaeobacter sp. strain Y4I. Applied and Environmental Microbiology 78 (14):4771–80. doi: 10.1128/AEM.00297-12.
   PubMed Web of Science ®Google Scholar
• de Silva, E. D., R. J. Andersen, and T. M. Allen. 1990. Geodiamolides C to F, new cytotoxic cyclodepsipeptides from the marine sponge Pseudaxinyssa sp. Tetrahedron Letters 31 (4):489–92. doi: 10.1016/0040-4039(90)87015-R.
   Web of Science ®Google Scholar
• DeFelice, S. L. 1995. The nutraceutical revolution: Its impact on food industry R&D. Trends in Food Science & Technology 6 (2):59–61. doi: 10.1016/S0924-2244(00)88944-X.
   Web of Science ®Google Scholar
• Dey, S. S., and K. C. Dora. 2014. Antioxidative activity of protein hydrolysate produced by alcalase hydrolysis from shrimp waste (Penaeus monodon and Penaeus indicus). Journal of Food Science and Technology 51 (3):449–57. doi: 10.1007/s13197-011-0512-z.
   PubMed Web of Science ®Google Scholar
• Ding, L.-J., W. Yuan, X.-J. Liao, B.-N. Han, S.-P. Wang, Z.-Y. Li, S.-H. Xu, W. Zhang, and H.-W. Lin. 2016. Oryzamides A-E, cyclodepsipeptides from the sponge-derived fungus Nigrospora oryzae PF18. Journal of Natural Products 79 (8):2045–52. doi: 10.1021/acs.jnatprod.6b00349.
   PubMed Web of Science ®Google Scholar
• Donia, M. S., B. Wang, D. C. Dunbar, P. V. Desai, A. Patny, M. Avery, and M. T. Hamann. 2008. Mollamides B and C, cyclic hexapeptides from the Indonesian tunicate Didemnum molle. Journal of Natural Products 71 (6):941–5. doi: 10.1021/np700718p.
   PubMed Web of Science ®Google Scholar
• Dorr, F. A., J. G. Kuhn, J. Phillips, and D. D. von Hoff. 1988. Phase I clinical and pharmacokinetic investigation of didemnin B, a cyclic depsipeptide. European Journal of Cancer & Clinical Oncology 24 (11):1699–706. doi: 10.1016/0277-5379(88)90070-3.
   PubMedGoogle Scholar
• Douglas, S. E., J. W. Gallant, R. S. Liebscher, A. Dacanay, and S. C. Tsoi. 2003. Identification and expression analysis of hepcidin-like antimicrobial peptides in bony fish. Developmental and Comparative Immunology 27 (6–7):589–601. doi: 10.1016/S0145-305X(03)00036-3.
   PubMed Web of Science ®Google Scholar
• Doyen, A., L. Beaulieu, L. Saucier, Y. Pouliot, and L. Bazinet. 2011. Impact of ultrafiltration membrane material on peptide separation from a snow crab byproduct hydrolysate by electrodialysis with ultrafiltration membranes. Journal of Agricultural and Food Chemistry 59 (5):1784–92. doi: 10.1021/jf103739m.
   PubMed Web of Science ®Google Scholar
• Dumez, H., E. Gallardo, S. Culine, J. C. Galceran, P. Schöffski, J. P. Droz, S. Extremera, S. Szyldergemajn, and A. Fléchon. 2009. Phase II study of biweekly plitidepsin as second-line therapy for advanced or metastatic transitional cell carcinoma of the urothelium. Marine Drugs 7 (3):451–63. doi: 10.3390/md7030451.
   PubMed Web of Science ®Google Scholar
• Edler, M. C., A. M. Fernandez, P. Lassota, C. M. Ireland, and L. R. Barrows. 2002. Inhibition of tubulin polymerization by vitilevuamide, a bicyclic marine peptide, at a site distinct from colchicine, the vinca alkaloids, and dolastatin 10. Biochemical Pharmacology 63 (4):707–15. doi: 10.1016/S0006-2952(01)00898-X.
   PubMed Web of Science ®Google Scholar
• El Maddah, F., S. Kehraus, M. Nazir, C. Almeida, and G. M. König. 2016. Insights into the biosynthetic origin of 3-(3-Furyl)alanine in Stachylidium sp. 293 K04 Tetrapeptides. Journal of Natural Products 79 (11):2838–45. doi: 10.1021/acs.jnatprod.6b00601.
   PubMed Web of Science ®Google Scholar
• Erdmann, K., B. W. Cheung, and H. Schröder. 2008. The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. The Journal of Nutritional Biochemistry 19 (10):643–54. doi: 10.1016/j.jnutbio.2007.11.010.
   PubMed Web of Science ®Google Scholar
• Fahmi, A., S. Morimura, H.-C. Guo, T. Shigematsu, K. Kida, and Y. Uemura. 2004. Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales. Process Biochemistry 39 (10):1195–200. doi: 10.1016/S0032-9592(03)00223-1.
   Web of Science ®Google Scholar
• Faivre, S., S. Chièze, C. Delbaldo, N. Ady-Vago, C. Guzman, L. Lopez-Lazaro, S. Lozahic, J. Jimeno, F. Pico, and J. P. Armand. 2005. Phase I and pharmacokinetic study of aplidine, a new marine cyclodepsipeptide in patients with advanced malignancies. Journal of Clinical Oncology. 23: 7871–7880.
   PubMed Web of Science ®Google Scholar
• Ford, P. W., K. R. Gustafson, T. C. McKee, N. Shigematsu, L. K. Maurizi, L. K. Pannell, D. E. Williams, E. Dilip de Silva, P. Lassota, T. M. Allen, et al. 1999. Papuamides A − D, HIV-inhibitory and cytotoxic depsipeptides from the Sponges Theonella m irabilis and Theonella s winhoei collected in Papua New Guinea. Journal of the American Chemical Society 121 (25):5899–909. doi: 10.1021/ja990582o.
   Web of Science ®Google Scholar
• Foster, M. P., G. P. Concepcion, G. B. Caraan, and C. M. Ireland. 1992. Bistratamides C and D. Two new oxazole-containing cyclic hexapeptides isolated from a Philippine Lissoclinum bistratum ascidian. The Journal of Organic Chemistry 57 (24):6671–5. doi: 10.1021/jo00050a063.
   Web of Science ®Google Scholar
• Fu, X., J. Su, and L. Zeng. 2000. Prepatellamide A, a new cyclic peptide from the ascidianLissoclinum patella. Science in China Series B: Chemistry 43 (6):643–8. doi: 10.1007/BF02969512.
   Google Scholar
• Fukuda, Y., T. Sugahara, M. Ueno, Y. Fukuta, Y. Ochi, K. Akiyama, T. Miyazaki, S. Masuda, A. Kawakubo, and K. Kato. 2006. The anti-tumor effect of Euchema serra agglutinin on colon cancer cells in vitro and in vivo. Anti-Cancer Drugs 17 (8):943–7. doi: 10.1097/01.cad.0000224458.13651.b4.
   PubMed Web of Science ®Google Scholar
• Gamble, W. R., N. A. Durso, R. W. Fuller, C. K. Westergaard, T. R. Johnson, D. L. Sackett, E. Hamel, J. H. Cardellina, and M. R. Boyd. 1999. Cytotoxic and tubulin-interactive hemiasterlins from Auletta sp. and Siphonochalina spp. sponges. Bioorganic & Medicinal Chemistry 7 (8):1611–5. doi: 10.1016/S0968-0896(99)00089-9.
   PubMed Web of Science ®Google Scholar
• Gao, J., and M. T. Hamann. 2011. Chemistry and biology of kahalalides. Chemical Reviews 111 (5):3208–35. doi: 10.1021/cr100187n.
   PubMed Web of Science ®Google Scholar
• Gao, X., Y. Liu, S. Kwong, Z. Xu, and T. Ye. 2010. Total synthesis and stereochemical reassignment of bisebromoamide. Organic Letters 12 (13):3018–21. doi: 10.1021/ol101021v.
   PubMed Web of Science ®Google Scholar
• García-Fernández, L. F., A. Losada, V. Alcaide, A. M. Alvarez, A. Cuadrado, L. González, K. Nakayama, K. I. Nakayama, J. M. Fernández-Sousa, A. Muñoz, et al. 2002. Aplidin induces the mitochondrial apoptotic pathway via oxidative stress-mediated JNK and p38 activation and protein kinase C delta. Oncogene 21 (49):7533–44. doi: 10.1038/sj.onc.1205972.
   PubMed Web of Science ®Google Scholar
• Garg, H. 1994. Bioactive substances in marine algae. In Nutrients and bioactive substances in aquatic organisms, eds. K. Devadasan, M. Mukundan, P. Antony, P. Viswanathan Nair, P. Perigreen, and J. Joseph, 16. Cochin, India: Society of Fisheries Technologists.
   Google Scholar
• Ghanbari, R., and A. Ebrahimpour. 2018. Separation and identification of bromelain-generated antibacterial peptides from Actinopyga lecanora. Food Science and Biotechnology 27 (2):591–8. doi: 10.1007/s10068-017-0267-z.
   PubMed Web of Science ®Google Scholar
• Giri, A., and T. Ohshima. 2012. Bioactive marine peptides: Nutraceutical value and novel approaches. Advances in Food and Nutrition Research 65:73–105. doi: 10.1016/B978-0-12-416003-3.00005-6.
   PubMedGoogle Scholar
• Gutiérrez, M., T. L. Suyama, N. Engene, J. S. Wingerd, T. Matainaho, and W. H. Gerwick. 2008. Apratoxin D, a potent cytotoxic cyclodepsipeptide from Papua New Guinea collections of the marine cyanobacteria Lyngbya majuscula and Lyngbya sordida. Journal of Natural Products 71 (6):1099–103. doi: 10.1021/np800121a.
   PubMed Web of Science ®Google Scholar
• Hamada, Y., and T. Shioiri. 2005. Recent progress of the synthetic studies of biologically active marine cyclic peptides and depsipeptides. Chemical Reviews 105 (12):4441–82. doi: 10.1021/cr0406312.
   PubMed Web of Science ®Google Scholar
• Hamann, M. T., C. S. Otto, P. J. Scheuer, and D. C. Dunbar. 1996. Kahalalides: Bioactive peptides from a marine mollusk Elysia rufescens and its algal diet Bryopsis sp.(1). The Journal of Organic Chemistry 61 (19):6594–600. doi: 10.1021/jo960877+.
   PubMed Web of Science ®Google Scholar
• Hambley, T. W., C. J. Hawkins, M. F. Lavin, A. van den Brenk, and D. J. Watters. 1992. Cycloxazoline: A cytotoxic cyclic hexapeptide from the ascidian lissoclinum bistratum. Tetrahedron 48 (2):341–8. doi: 10.1016/S0040-4020(01)88146-1.
   Web of Science ®Google Scholar
• Han, B., H. Gross, K. L. McPhail, D. Goeger, C. S. Maier, and W. H. Gerwick. 2011. Wewakamide A and guineamide G, cyclic depsipeptides from the marine cyanobacteria Lyngbya semiplena and Lyngbya majuscula. Journal of Microbiology and Biotechnology 21 (9):930–6. doi: 10.4014/jmb.1105.05011.
   PubMed Web of Science ®Google Scholar
• Harada, K., T. Maeda, Y. Hasegawa, T. Tokunaga, Y. Tamura, and T. Koizumi. 2010. Antioxidant activity of fish sauces including puffer (Lagocephalus wheeleri) fish sauce measured by the oxygen radical absorbance capacity method. Molecular Medicine Reports 3 (4):663–8. doi: 10.3892/mmr_00000313.
   PubMed Web of Science ®Google Scholar
• Harnedy, P. A., and R. J. FitzGerald. 2011. Bioactive proteins, peptides, and amino acids from macroalgae(1). Journal of Phycology 47 (2):218–32. doi: 10.1111/j.1529-8817.2011.00969.x.
   PubMed Web of Science ®Google Scholar
• Hori, K., S. Ikegami, K. Miyazawa, and K. Ito. 1988. Mitogenic and antineoplastic isoagglutinins from the red alga Solieria robusta. Phytochemistry 27 (7):2063–7. doi: 10.1016/0031-9422(88)80097-9.
   Web of Science ®Google Scholar
• Hori, K., K. Matsubara, and K. Miyazawa. 2000. Primary structures of two hemagglutinins from the marine red alga, Hypnea japonica. Biochimica et Biophysica Acta (Bba) - General Subjects 1474 (2):226–36. doi: 10.1016/S0304-4165(00)00008-8.
   PubMed Web of Science ®Google Scholar
• Hsu, K.-C., E. C. Li-Chan, and C.-L. Jao. 2011. Antiproliferative activity of peptides prepared from enzymatic hydrolysates of tuna dark muscle on human breast cancer cell line MCF-7. Food Chemistry 126 (2):617–22. doi: 10.1016/j.foodchem.2010.11.066.
   Web of Science ®Google Scholar
• Isaka, M., U. Srisanoh, N. Lartpornmatulee, and T. Boonruangprapa. 2007. ES-242 derivatives and cycloheptapeptides from Cordyceps sp. strains BCC 16173 and BCC 16176. Journal of Natural Products 70 (10):1601–4. doi: 10.1021/np070357h.
   PubMed Web of Science ®Google Scholar
• Je, J.-Y., J.-Y. Park, W.-K. Jung, P.-J. Park, and S.-K. Kim. 2005a. Isolation of angiotensin I converting enzyme (ACE) inhibitor from fermented oyster sauce, Crassostrea gigas. Food Chemistry 90 (4):809–14. doi: 10.1016/j.foodchem.2004.05.028.
   Web of Science ®Google Scholar
• Je, J.-Y., P.-J. Park, and S.-K. Kim. 2005b. Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Food Research International 38 (1):45–50. doi: 10.1016/j.foodres.2004.07.005.
   Web of Science ®Google Scholar
• Je, J.-Y., Z.-J. Qian, H.-G. Byun, and S.-K. Kim. 2007. Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis. Process Biochemistry 42 (5):840–6. doi: 10.1016/j.procbio.2007.02.006.
   Web of Science ®Google Scholar
• Je, J.-Y., Z.-J. Qian, S.-H. Lee, H.-G. Byun, and S.-K. Kim. 2008. Purification and antioxidant properties of bigeye tuna (Thunnus obesus) dark muscle peptide on free radical-mediated oxidative systems. Journal of Medicinal Food 11 (4):629–37. doi: 10.1089/jmf.2007.0114.
   PubMed Web of Science ®Google Scholar
• Jo, H.-Y., W.-K. Jung, and S.-K. Kim. 2008. Purification and characterization of a novel anticoagulant peptide from marine echiuroid worm, Urechis unicinctus. Process Biochemistry 43 (2):179–84. doi: 10.1016/j.procbio.2007.11.011.
   Web of Science ®Google Scholar
• Jo, C., F. F. Khan, M. I. Khan, and J. Iqbal. 2017. Marine bioactive peptides: Types, structures, and physiological functions. Food Reviews International 33 (1):44–61. doi: 10.1080/87559129.2015.1137311.
   Web of Science ®Google Scholar
• Jun, S.-Y., P.-J. Park, W.-K. Jung, and S.-K. Kim. 2004. Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. European Food Research and Technology 219 (1):20–6. doi: 10.1007/s00217-004-0882-9.
   Web of Science ®Google Scholar
• Jung, W.-K., R. Karawita, S.-J. Heo, B.-J. Lee, S.-K. Kim, and Y.-J. Jeon. 2006a. Recovery of a novel Ca-binding peptide from Alaska Pollack (Theragra chalcogramma) backbone by pepsinolytic hydrolysis. Process Biochemistry 41 (9):2097–100. doi: 10.1016/j.procbio.2006.05.008.
   Web of Science ®Google Scholar
• Jung, W.-K., and S.-K. Kim. 2007. Calcium-binding peptide derived from pepsinolytic hydrolysates of hoki (Johnius belengerii) frame. European Food Research and Technology 224 (6):763–7. doi: 10.1007/s00217-006-0371-4.
   Web of Science ®Google Scholar
• Jung, W.-K., E. Mendis, J.-Y. Je, P.-J. Park, B. W. Son, H. C. Kim, Y. K. Choi, and S.-K. Kim. 2006b. Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats. Food Chemistry 94 (1):26–32. doi: 10.1016/j.foodchem.2004.09.048.
   Web of Science ®Google Scholar
• Jung, W.-K., Z.-J. Qian, S.-H. Lee, S. Y. Choi, N. J. Sung, H.-G. Byun, and S.-K. Kim. 2007. Free radical scavenging activity of a novel antioxidative peptide isolated from in vitro gastrointestinal digests of Mytilus coruscus. Journal of Medicinal Food 10 (1):197–202. doi: 10.1089/jmf.2006.101.
   PubMed Web of Science ®Google Scholar
• Kalemkerian, G. P., X. Ou, M. R. Adil, R. Rosati, M. M. Khoulani, S. K. Madan, and G. R. Pettit. 1999. Activity of dolastatin 10 against small-cell lung cancer in vitro and in vivo: Induction of apoptosis and bcl-2 modification. Cancer Chemotherapy and Pharmacology 43 (6):507–15. doi: 10.1007/s002800050931.
   PubMed Web of Science ®Google Scholar
• Kannel, W., and M. Higgins. 1990. Smoking and hypertension as predictors of cardiovascular risk in population studies. Journal of Hypertension. Supplement: Official Journal of the International Society of Hypertension 8:S3–S8.
   PubMedGoogle Scholar
• Khan, B. M., and Y. Liu. 2019. Marine mollusks: Food with benefits. Comprehensive Reviews in Food Science and Food Safety 18 (2):548–64. doi: 10.1111/1541-4337.12429.
   PubMed Web of Science ®Google Scholar
• Kim, S.-Y., J.-Y. Je, and S.-K. Kim. 2007. Purification and characterization of antioxidant peptide from hoki (Johnius belengerii) frame protein by gastrointestinal digestion. The Journal of Nutritional Biochemistry 18 (1):31–8. doi: 10.1016/j.jnutbio.2006.02.006.
   PubMed Web of Science ®Google Scholar
• Kobayashi, M., S. Aoki, N. Ohyabu, M. Kurosu, W. Wang, and I. Kitagawa. 1994. Arenastatin A, a potent cytotoxic depsipeptide from the Okinawan marine sponge Dysidea arenaria. Tetrahedron Letters 35 (41):7969–72. doi: 10.1016/S0040-4039(00)78398-5.
   Google Scholar
• Kristinsson, H. G., and H. O. Hultin. 2003. Effect of low and high pH treatment on the functional properties of cod muscle proteins. Journal of Agricultural and Food Chemistry 51 (17):5103–10. doi: 10.1021/jf026138d.
   PubMed Web of Science ®Google Scholar
• Kristinsson, H. G., and B. Ingadottir. 2006. Recovery and properties of muscle proteins extracted from tilapia (Oreochromis niloticus) light muscle by pH shift processing. Journal of Food Science 71 (3):E132–E141. doi: 10.1111/j.1365-2621.2006.tb15626.x.
   Web of Science ®Google Scholar
• Kristinsson, H. G., A. E. Theodore, N. Demir, and B. Ingadottir. 2006. A comparative study between acid‐and alkali‐aided processing and surimi processing for the recovery of proteins from channel catfish muscle. Journal of Food Science 70 (4):C298–C306. doi: 10.1111/j.1365-2621.2005.tb07177.x.
   Web of Science ®Google Scholar
• Kucuk, O., M. L. Young, T. M. Habermann, B. C. Wolf, J. Jimeno, and P. A. Cassileth. 2000. Phase II trail of didemnin B in previously treated non-Hodgkin's lymphoma: an Eastern Cooperative Oncology Group (ECOG) Study. American Journal of Clinical Oncology 23 (3):273–7. doi: 10.1097/00000421-200006000-00013.
   PubMed Web of Science ®Google Scholar
• Kumar, N. S., R. Nazeer, and R. Jaiganesh. 2011. Purification and biochemical characterization of antioxidant peptide from horse mackerel (Magalaspis cordyla) viscera protein. Peptides 32 (7):1496–501. doi: 10.1016/j.peptides.2011.05.020.
   PubMed Web of Science ®Google Scholar
• Lee, J. K., S. Hong, J.-K. Jeon, S.-K. Kim, and H.-G. Byun. 2009. Purification and characterization of angiotensin I converting enzyme inhibitory peptides from the rotifer, Brachionus rotundiformis. Bioresource Technology 100 (21):5255–9. doi: 10.1016/j.biortech.2009.05.057.
   PubMed Web of Science ®Google Scholar
• Lee, J.-W., and T. W. Jeffries. 2011. Efficiencies of acid catalysts in the hydrolysis of lignocellulosic biomass over a range of combined severity factors. Bioresource Technology 102 (10):5884–90. doi: 10.1016/j.biortech.2011.02.048.
   PubMed Web of Science ®Google Scholar
• Lee, T.-G., and S. Maruyama. 1998. Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. Biochemical and Biophysical Research Communications 253 (3):604–8. doi: 10.1006/bbrc.1998.9824.
   PubMed Web of Science ®Google Scholar
• Lee, J.-Y., B. Orlikova, and M. Diederich. 2015. Signal transducers and activators of transcription (STAT) regulatory networks in marine organisms: From physiological observations towards marine drug discovery. Marine Drugs 13 (8):4967–84. doi: 10.3390/md13084967.
   PubMed Web of Science ®Google Scholar
• Lee, Y., C. Phat, and S.-C. Hong. 2017. Structural diversity of marine cyclic peptides and their molecular mechanisms for anticancer, antibacterial, antifungal, and other clinical applications. Peptides 95:94–105. doi: 10.1016/j.peptides.2017.06.002.
   PubMed Web of Science ®Google Scholar
• Lee, S.-H., Z.-J. Qian, and S.-K. Kim. 2010. A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats. Food Chemistry 118 (1):96–102. doi: 10.1016/j.foodchem.2009.04.086.
   Web of Science ®Google Scholar
• Liang, X., X.-Y. Zhang, X.-H. Nong, J. Wang, Z.-H. Huang, and S.-H. Qi. 2016. Eight linear peptides from the deep-sea-derived fungus Simplicillium obclavatum EIODSF 020. Tetrahedron 72 (22):3092–7. doi: 10.1016/j.tet.2016.04.032.
   Web of Science ®Google Scholar
• Li, G.-H., G.-W. Le, Y.-H. Shi, and S. Shrestha. 2004. Angiotensin I–converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutrition Research 24 (7):469–86. doi: 10.1016/S0271-5317(04)00058-2.
   Web of Science ®Google Scholar
• Ling, Y.-H., M. Aracil, J. Jimeno, R. Perez-Soler, and Y. Zou. 2009. Molecular pharmacodynamics of PM02734 (elisidepsin) as single agent and in combination with erlotinib; synergistic activity in human non-small cell lung cancer cell lines and xenograft models. European Journal of Cancer (Oxford, England : 1990) 45 (10):1855–64. doi: 10.1016/j.ejca.2009.03.003.
   PubMed Web of Science ®Google Scholar
• Lin, Z., C. A. Reilly, R. Antemano, R. W. Hughen, L. Marett, G. P. Concepcion, M. G. Haygood, B. M. Olivera, A. Light, and E. W. Schmidt. 2011. Nobilamides A-H, long-acting transient receptor potential vanilloid-1 (TRPV1) antagonists from mollusk-associated bacteria . Journal of Medicinal Chemistry 54 (11):3746–55. doi: 10.1021/jm101621u.
   PubMed Web of Science ®Google Scholar
• Liu, S., Y.-M. Cui, and F.-J. Nan. 2008a. Total synthesis of the originally proposed and revised structures of scleritodermin A. Organic Letters 10 (17):3765–8. doi: 10.1021/ol801419m.
   PubMed Web of Science ®Google Scholar
• Liu, Z., S. Dong, J. Xu, M. Zeng, H. Song, and Y. Zhao. 2008b. Production of cysteine-rich antimicrobial peptide by digestion of oyster (Crassostrea gigas) with alcalase and bromelin. Food Control 19 (3):231–5. doi: 10.1016/j.foodcont.2007.03.004.
   Web of Science ®Google Scholar
• Liu, L., and K. S. Rein. 2010. New peptides isolated from Lyngbya species: A review. Marine Drugs 8 (6):1817–37. doi: 10.3390/md8061817.
   PubMed Web of Science ®Google Scholar
• Li, W.-L., Y.-H. Yi, H.-M. Wu, Q.-Z. Xu, H.-F. Tang, D.-Z. Zhou, H.-W. Lin, and Z.-H. Wang. 2003. Isolation and structure of the cytotoxic cycloheptapeptide phakellistatin 13. Journal of Natural Products 66 (1):146–8. doi: 10.1021/np020223y.
   PubMed Web of Science ®Google Scholar
• Li, Y., and J. Yu. 2015. Research progress in structure-activity relationship of bioactive peptides. Journal of Medicinal Food 18 (2):147–56. doi: 10.1089/jmf.2014.0028.
   PubMed Web of Science ®Google Scholar
• Loganzo, F., C. M. Discafani, T. Annable, C. Beyer, S. Musto, M. Hari, X. Tan, C. Hardy, R. Hernandez, M. Baxter, et al. 2003. HTI-286, a synthetic analogue of the tripeptide hemiasterlin, is a potent antimicrotubule agent that circumvents P-glycoprotein-mediated resistance in vitro and in vivo. Cancer Research 63 (8):1838–45.
   PubMed Web of Science ®Google Scholar
• Loow, Y.-L., T. Y. Wu, J. M. Jahim, A. W. Mohammad, and W. H. Teoh. 2016. Typical conversion of lignocellulosic biomass into reducing sugars using dilute acid hydrolysis and alkaline pretreatment. Cellulose 23 (3):1491–520. doi: 10.1007/s10570-016-0936-8.
   Web of Science ®Google Scholar
• Ma, D., B. Zou, G. Cai, X. Hu, and J. O. Liu. 2006. Total synthesis of the cyclodepsipeptide apratoxin A and its analogues and assessment of their biological activities. Chemistry (Weinheim an der Bergstrasse, Germany) 12 (29):7615–26. doi: 10.1002/chem.200600599.
   PubMed Web of Science ®Google Scholar
• MacMillan, J. B., M. A. Ernst-Russell, J. S. De Ropp, and T. F. Molinski. 2002. Lobocyclamides A − C, Lipopeptides from a cryptic cyanobacterial mat containing Lyngbya c onfervoides. The Journal of Organic Chemistry 67 (23):8210–5. doi: 10.1021/jo0261909.
   PubMed Web of Science ®Google Scholar
• Madden, T., H. T. Tran, D. Beck, R. Huie, R. A. Newman, L. Pusztai, J. J. Wright, and J. L. Abbruzzese. 2000. Novel marine-derived anticancer agents: A phase I clinical, pharmacological, and pharmacodynamic study of dolastatin 10 (NSC 376128) in patients with advanced solid tumors. Clinical Cancer Research 6:1293–301.
   PubMed Web of Science ®Google Scholar
• Malaker, A., and S. A. I. Ahmad. 2013. Therapeutic potency of anticancer peptides derived from marine organism. International Journal of Engineering 2:2305–8269.
   Google Scholar
• Marcos, B., T. Aymerich, J. M. Monfort, and M. Garriga. 2008. High-pressure processing and antimicrobial biodegradable packaging to control Listeria monocytogenes during storage of cooked ham. Food Microbiology 25 (1):177–82. doi: 10.1016/j.fm.2007.05.002.
   PubMed Web of Science ®Google Scholar
• Marquez, B. L., K. S. Watts, A. Yokochi, M. A. Roberts, P. Verdier-Pinard, J. I. Jimenez, E. Hamel, P. J. Scheuer, and W. H. Gerwick. 2002. Structure and absolute stereochemistry of hectochlorin, a potent stimulator of actin assembly. Journal of Natural Products 65 (6):866–71. doi: 10.1021/np0106283.
   PubMed Web of Science ®Google Scholar
• Mateos, M. V., M. T. Cibeira, P. G. Richardson, F. Prosper, A. Oriol, J. de la Rubia, J. J. Lahuerta, R. García-Sanz, S. Extremera, S. Szyldergemajn, et al. 2010. Phase II clinical and pharmacokinetic study of plitidepsin 3-hour infusion every two weeks alone or with dexamethasone in relapsed and refractory multiple myeloma. Clinical Cancer Research: An Official Journal of the American Association for Cancer Research 16 (12):3260–9. doi: 10.1158/1078-0432.CCR-10-0469.
   PubMed Web of Science ®Google Scholar
• Matsunaga, S., and N. Fusetani. 2003. Nonribosomal peptides from marine sponges. Current Organic Chemistry 7 (10):945–66. doi: 10.2174/1385272033486648.
   Web of Science ®Google Scholar
• Matsunaga, S., N. Fusetani, and S. Konosu. 1984. Bioactive marine metabolites VI. Structure elucidation of discodermin A, an antimicrobial peptide from the marine sponge Discodermia kiiensis. Tetrahedron Letters 25 (45):5165–8. doi: 10.1016/S0040-4039(01)81553-7.
   Web of Science ®Google Scholar
• Matsunaga, S., N. Fusetani, and S. Konosu. 1985. Bioactive marine metabolites VII. Structures of discodermins B, C, and D, antimicrobial peptides from the marine sponge discodermia kiiensis. Tetrahedron Letters 26 (7):855–6. doi: 10.1016/S0040-4039(00)61947-0.
   Web of Science ®Google Scholar
• Mayer, A. M., K. B. Glaser, C. Cuevas, R. S. Jacobs, W. Kem, R. D. Little, J. M. McIntosh, D. J. Newman, B. C. Potts, and D. E. Shuster. 2010. The odyssey of marine pharmaceuticals: A current pipeline perspective. Trends in Pharmacological Sciences 31 (6):255–65. doi: 10.1016/j.tips.2010.02.005.
   PubMed Web of Science ®Google Scholar
• McIntosh, M., L. Cruz, M. Hunkapiller, W. Gray, and B. Olivera. 1982. Isolation and structure of a peptide toxin from the marine snail Conus magus. Archives of Biochemistry and Biophysics 218 (1):329–34. doi: 10.1016/0003-9861(82)90351-4.
   PubMed Web of Science ®Google Scholar
• Mechnich, O., and H. Kessler. 1997. What are the structures of phakellistatin 2 and phakellistatin 4? Letters in Peptide Science 4 (1):21–8. doi: 10.1007/BF02443551.
   Google Scholar
• Medina, R. A., D. E. Goeger, P. Hills, S. L. Mooberry, N. Huang, L. I. Romero, E. Ortega-Barría, W. H. Gerwick, and K. L. McPhail. 2008. Coibamide A, a potent antiproliferative cyclic depsipeptide from the Panamanian marine cyanobacterium Leptolyngbya sp. Journal of the American Chemical Society 130 (20):6324–5. doi: 10.1021/ja801383f.
   PubMed Web of Science ®Google Scholar
• Mendis, E., N. Rajapakse, H.-G. Byun, and S.-K. Kim. 2005a. Investigation of jumbo squid (Dosidicus gigas) skin gelatin peptides for their in vitro antioxidant effects. Life Sciences 77 (17):2166–78. doi: 10.1016/j.lfs.2005.03.016.
   PubMed Web of Science ®Google Scholar
• Mendis, E., N. Rajapakse, and S.-K. Kim. 2005b. Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. Journal of Agricultural and Food Chemistry 53 (3):581–7. doi: 10.1021/jf048877v.
   PubMed Web of Science ®Google Scholar
• Miguel, M., M. Contreras, I. Recio, and A. Aleixandre. 2009. ACE-inhibitory and antihypertensive properties of a bovine casein hydrolysate. Food Chemistry 112 (1):211–4. doi: 10.1016/j.foodchem.2008.05.041.
   Web of Science ®Google Scholar
• Miljanich, G. 2004. Ziconotide: Neuronal calcium channel blocker for treating severe chronic pain. Current Medicinal Chemistry 11 (23):3029–40. doi: 10.2174/0929867043363884.
   PubMed Web of Science ®Google Scholar
• Mittelman, A., H. G. Chun, C. Puccio, N. Coombe, T. Lansen, and T. Ahmed. 1999. Phase II clinical trial of didemnin B in patients with recurrent or refractory anaplastic astrocytoma or glioblastoma multiforme (NSC 325319). Investigational New Drugs 17 (2):179–82. doi: 10.1023/a:1006379402114.
   PubMed Web of Science ®Google Scholar
• Möller, N. P., K. E. Scholz-Ahrens, N. Roos, and J. Schrezenmeir. 2008. Bioactive peptides and proteins from foods: Indication for health effects. European Journal of Nutrition 47 (4):171–82. doi: 10.1007/s00394-008-0710-2.
   PubMed Web of Science ®Google Scholar
• Mooberry, S. L., R. M. Leal, T. L. Tinley, H. Luesch, R. E. Moore, and T. H. Corbett. 2003. The molecular pharmacology of symplostatin 1: A new antimitotic dolastatin 10 analog. International Journal of Cancer 104 (4):512–21. doi: 10.1002/ijc.10982.
   PubMed Web of Science ®Google Scholar
• Najafian, L., and A. Babji. 2012. A review of fish-derived antioxidant and antimicrobial peptides: Their production, assessment, and applications. Peptides 33 (1):178–85. doi: 10.1016/j.peptides.2011.11.013.
   PubMed Web of Science ®Google Scholar
• Nakagomi, K., A. Fujimura, H. Ebisu, T. Sakai, Y. Sadakane, N. Fujii, and T. Tanimura. 1998. Acein-1, a novel angiotensin-I-converting enzyme inhibitory peptide isolated from tryptic hydrolysate of human plasma. FEBS Letters 438 (3):255–7. doi: 10.1016/s0014-5793(98)01311-8.
   PubMed Web of Science ®Google Scholar
• Nakagomi, K., R. Yamada, H. Ebisu, Y. Sadakane, T. Akizawa, and T. Tanimura. 2000. Isolation of Acein-2, a novel angiotensin-I-converting enzyme inhibitory peptide derived from a tryptic hydrolysate of human plasma. FEBS Letters 467 (2–3):235–8. doi: 10.1016/s0014-5793(00)01163-7.
   PubMed Web of Science ®Google Scholar
• Nakashima, Y., Y. Egami, M. Kimura, T. Wakimoto, and I. Abe. 2016. Metagenomic analysis of the sponge Discodermia reveals the production of the cyanobacterial natural product kasumigamide by 'Entotheonella'. PLoS One 11 (10):e0164468. doi: 10.1371/journal.pone.0164468.
   PubMed Web of Science ®Google Scholar
• Newman, D. J., and G. M. Cragg. 2004. Advanced preclinical and clinical trials of natural products and related compounds from marine sources. Current Medicinal Chemistry 11 (13):1693–713. doi: 10.2174/0929867043364982.
   PubMed Web of Science ®Google Scholar
• Newman, D. J., and G. M. Cragg. 2014. Marine-sourced anti-cancer and cancer pain control agents in clinical and late preclinical development. Marine Drugs 12 (1):255–78. doi: 10.3390/md12010255.
   PubMed Web of Science ®Google Scholar
• Ngo, D.-H., and S.-K. Kim. 2013. Marine bioactive peptides as potential antioxidants. Current Protein & Peptide Science 14 (3):189–98. doi: 10.2174/13892037113149990041.
   PubMed Web of Science ®Google Scholar
• Ngo, D.-H., T.-S. Vo, D.-N. Ngo, I. Wijesekara, and S.-K. Kim. 2012. Biological activities and potential health benefits of bioactive peptides derived from marine organisms. International Journal of Biological Macromolecules 51 (4):378–83. doi: 10.1016/j.ijbiomac.2012.06.001.
   PubMed Web of Science ®Google Scholar
• Nielsen, C. K., R. J. Lewis, D. Alewood, R. Drinkwater, E. Palant, M. Patterson, T. L. Yaksh, D. McCumber, and M. T. Smith. 2005. Anti-allodynic efficacy of the chi-conopeptide, Xen2174, in rats with neuropathic pain. Pain 118 (1–2):112–24. doi: 10.1016/j.pain.2005.08.002.
   PubMed Web of Science ®Google Scholar
• Nogle, L. M., B. L. Marquez, and W. H. Gerwick. 2003. Wewakazole, a novel cyclic dodecapeptide from a Papua New Guinea Lyngbya m ajuscula. Organic Letters 5 (1):3–6. doi: 10.1021/ol026811k.
   PubMed Web of Science ®Google Scholar
• Odaka, C., M. L. Sanders, and P. Crews. 2000. Jasplakinolide induces apoptosis in various transformed cell lines by a caspase-3-like protease-dependent pathway. Clinical and Diagnostic Laboratory Immunology 7 (6):947–52. doi: 10.1128/cdli.7.6.947-952.2000.
   PubMedGoogle Scholar
• Oku, N., K. R. Gustafson, L. K. Cartner, J. A. Wilson, N. Shigematsu, S. Hess, L. K. Pannell, M. R. Boyd, and J. B. McMahon. 2004. Neamphamide A, a new HIV-inhibitory depsipeptide from the Papua New Guinea marine sponge Neamphius huxleyi. Journal of Natural Products 67 (8):1407–11. doi: 10.1021/np040003f.
   PubMed Web of Science ®Google Scholar
• Oku, N., R. Krishnamoorthy, A. G. Benson, R. L. Ferguson, M. A. Lipton, L. R. Phillips, K. R. Gustafson, and J. B. McMahon. 2005. Complete stereochemistry of neamphamide A and absolute configuration of the beta-methoxytyrosine residue in papuamide B. The Journal of Organic Chemistry 70 (17):6842–7. doi: 10.1021/jo0508853.
   PubMed Web of Science ®Google Scholar
• Olivera, B. M., W. R. Gray, R. Zeikus, J. M. McIntosh, J. Varga, J. Rivier, V. De Santos, and L. J. Cruz. 1985. Peptide neurotoxins from fish-hunting cone snails. Science (New York, N.Y.) 230 (4732):1338–43. doi: 10.1126/science.4071055.
   PubMed Web of Science ®Google Scholar
• Ott, P. A., O. Hamid, A. C. Pavlick, H. Kluger, K. B. Kim, P. D. Boasberg, R. Simantov, E. Crowley, J. A. Green, T. Hawthorne, et al. 2014. Phase I/II study of the antibody-drug conjugate glembatumumab vedotin in patients with advanced melanoma. Journal of Clinical Oncology: Official Journal of the American Society of Clinical Oncology 32 (32):3659–66. doi: 10.1200/JCO.2013.54.8115.
   PubMed Web of Science ®Google Scholar
• Ovissipour, M., A. Abedian, A. Motamedzadegan, B. Rasco, R. Safari, and H. Shahiri. 2009. The effect of enzymatic hydrolysis time and temperature on the properties of protein hydrolysates from Persian sturgeon (Acipenser persicus) viscera. Food Chemistry 115 (1):238–42. doi: 10.1016/j.foodchem.2008.12.013.
   Web of Science ®Google Scholar
• Pelay-Gimeno, M., A. Meli, J. Tulla-Puche, and F. Albericio. 2013. Rescuing biological activity from synthetic phakellistatin 19. Journal of Medicinal Chemistry 56 (23):9780–8. doi: 10.1021/jm401520x.
   PubMed Web of Science ®Google Scholar
• Perez Espitia, P. J., N. de Fátima Ferreira Soares, J. S. dos Reis Coimbra, N. J. de Andrade, R. Souza Cruz, and E. A. A. Medeiros. 2012. Bioactive peptides: Synthesis, properties, and applications in the packaging and preservation of food. Comprehensive Reviews in Food Science and Food Safety 11 (2):187–204. doi: 10.1111/j.1541-4337.2011.00179.x.
   PubMed Web of Science ®Google Scholar
• Pettit, G. R., Z. Cichacz, J. Barkoczy, A.-C. Dorsaz, D. L. Herald, M. D. Williams, D. L. Doubek, J. M. Schmidt, L. P. Tackett, and D. C. Brune. 1993. Isolation and structure of the marine sponge cell growth inhibitory cyclic peptide phakellistatin 1. Journal of Natural Products 56 (2):260–7. doi: 10.1021/np50092a011.
   PubMed Web of Science ®Google Scholar
• Pettit, G. R., M. R. Rhodes, and R. Tan. 1999. Antineoplastic Agents. 400. Synthesis of the Indian Ocean marine sponge cyclic heptapeptide Phakellistatin 2, 1a. Journal of Natural Products 62 (3):409–14. doi: 10.1021/np980168m.
   PubMed Web of Science ®Google Scholar
• Pettit, G. R., S. B. Singh, F. Hogan, P. Lloyd-Williams, D. L. Herald, D. D. Burkett, and P. J. Clewlow. 1989. Antineoplastic agents. Part 189. The absolute configuration and synthesis of natural (-)-dolastatin 10. Journal of the American Chemical Society 111 (14):5463–5. doi: 10.1021/ja00196a061.
   Web of Science ®Google Scholar
• Pettit, G. R., and R. Tan. 2003. Antineoplastic agents 390. Isolation and structure of phakellistatin 12 from a Chuuk archipelago marine sponge. Bioorganic & Medicinal Chemistry Letters 13 (4):685–8. doi: 10.1016/S0960-894X(02)01054-5.
   PubMed Web of Science ®Google Scholar
• Pettit, G. R., and R. Tan. 2005. Isolation and structure of Phakellistatin 14 from the Western Pacific marine sponge Phakellia sp., 1. Journal of Natural Products 68 (1):60–3. doi: 10.1021/np040092w.
   PubMed Web of Science ®Google Scholar
• Pettit, G. R., R. Tan, D. L. Herald, M. D. Williams, and R. L. Cerny. 1994a. Antineoplastic agents. 277. Isolation and structure of phakellistatin 3 and isophakellistatin 3 from a Republic of Comoros marine sponge. The Journal of Organic Chemistry 59 (7):1593–5. doi: 10.1021/jo00086a001.
   Web of Science ®Google Scholar
• Pettit, G. R., R. Tan, Y. Ichihara, M. D. Williams, D. L. Doubek, L. P. Tackett, J. M. Schmidt, R. L. Cerny, M. R. Boyd, and J. N. Hooper. 1995a. Antineoplastic agents, 325. Isolation and structure of the human cancer cell growth inhibitory cyclic octapeptides phakellistatin 10 and 11 from Phakellia sp. Journal of Natural Products 58 (6):961–5. doi: 10.1021/np50120a025.
   PubMed Web of Science ®Google Scholar
• Pettit, G. R., J.-P. Xu, Z. Cichacz, J. M. Achmidt, A.-C. Dorsaz, M. R. Boyd, and R. L. Cerny. 1995b. Isolation and structure of the human cancer cell growth inhibitory phakellistatin 4 from the western Pacific sponge Phakellia costata. Heterocycles 40 (2):501–6. doi: 10.3987/COM-94-S45.
   Web of Science ®Google Scholar
• Pettit, G. R., J.-P. Xu, Z. A. Cichacz, M. D. Williams, J.-C. Chapuis, and R. L. Cerny. 1994b. Antineoplastic agents 323. Isolation and structure of phakellistatin 6 from a Chuuk archipelago marine sponge. Bioorganic & Medicinal Chemistry Letters 4 (22):2677–82. doi: 10.1016/S0960-894X(01)80695-8.
   Web of Science ®Google Scholar
• Pettit, G. R., J.-p. Xu, Z. A. Cichacz, M. D. Williams, A.-C. Dorsaz, D. C. Brune, M. R. Boyd, and R. L. Cerny. 1994c. Antineoplastic agents 315. Isolation and structure of the marine sponge cancer cell growth inhibitor phakellistatin 5. Bioorganic & Medicinal Chemistry Letters 4 (17):2091–6. doi: 10.1016/S0960-894X(01)80108-6.
   Web of Science ®Google Scholar
• Pettit, G. R., J.-p. Xu, A.-C. Dorsaz, M. D. Williams, M. R. Boyd, and R. L. Cerny. 1995c. Isolation and structure of the human cancer cell growth inhibitory cyclic decapeptides phakellistatins 7, 8 and 91, 2. Bioorganic & Medicinal Chemistry Letters 5 (13):1339–44. doi: 10.1016/0960-894X(95)00219-J.
   Web of Science ®Google Scholar
• Picot, L., S. Bordenave, S. Didelot, I. Fruitier-Arnaudin, F. Sannier, G. Thorkelsson, J. Bergé, F. Guérard, A. Chabeaud, and J. Piot. 2006. Antiproliferative activity of fish protein hydrolysates on human breast cancer cell lines. Process Biochemistry 41 (5):1217–22. doi: 10.1016/j.procbio.2005.11.024.
   Web of Science ®Google Scholar
• Plaza, A., G. Bifulco, J. L. Keffer, J. R. Lloyd, H. L. Baker, and C. A. Bewley. 2009. Celebesides A − C and theopapuamides B − D, depsipeptides from an Indonesian sponge that inhibit HIV-1 entry. The Journal of Organic Chemistry 74 (2):504–12. doi: 10.1021/jo802232u.
   PubMed Web of Science ®Google Scholar
• Plaza, A., E. Gustchina, H. L. Baker, M. Kelly, and C. A. Bewley. 2007. Mirabamides A–D, depsipeptides from the sponge Siliquariaspongia mirabilis that inhibit HIV-1 fusion. Journal of Natural Products 70 (11):1753–60. doi: 10.1021/np070306k.
   PubMed Web of Science ®Google Scholar
• Plummer, R., P. Lorigan, E. Brown, R. Zaucha, V. Moiseyenko, L. Demidov, V. Soriano, E. Chmielowska, R. Andrés, G. Kudryavtseva, et al. 2013. Phase I-II study of plitidepsin and dacarbazine as first-line therapy for advanced melanoma. British Journal of Cancer 109 (6):1451–9. doi: 10.1038/bjc.2013.477.
   PubMed Web of Science ®Google Scholar
• Pomponi, S. A. 2001. The Rogar Revelle commemorative lecture: The oceans and human health: The discovery and development of marine-derived drugs. Oceanography 14 (1):78–87. doi: 10.5670/oceanog.2001.53.
   Google Scholar
• Qian, Z.-J., J.-Y. Je, and S.-K. Kim. 2007. Antihypertensive effect of angiotensin I converting enzyme-inhibitory peptide from hydrolysates of bigeye tuna dark muscle, Thunnus obesus. Journal of Agricultural and Food Chemistry 55 (21):8398–403. doi: 10.1021/jf0710635.
   PubMed Web of Science ®Google Scholar
• Qian, Z.-J., W.-K. Jung, H.-G. Byun, and S.-K. Kim. 2008. Protective effect of an antioxidative peptide purified from gastrointestinal digests of oyster, Crassostrea gigas against free radical induced DNA damage. Bioresource Technology 99 (9):3365–71. doi: 10.1016/j.biortech.2007.08.018.
   PubMed Web of Science ®Google Scholar
• Rajapakse, N., E. Mendis, H.-G. Byun, and S.-K. Kim. 2005a. Purification and in vitro antioxidative effects of giant squid muscle peptides on free radical-mediated oxidative systems. The Journal of Nutritional Biochemistry 16 (9):562–9. doi: 10.1016/j.jnutbio.2005.02.005.
   PubMed Web of Science ®Google Scholar
• Rajapakse, N., E. Mendis, W.-K. Jung, J.-Y. Je, and S.-K. Kim. 2005b. Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties. Food Research International 38 (2):175–82. doi: 10.1016/j.foodres.2004.10.002.
   Web of Science ®Google Scholar
• Ranathunga, S., N. Rajapakse, and S.-K. Kim. 2006. Purification and characterization of antioxidative peptide derived from muscle of conger eel (Conger myriaster). European Food Research and Technology 222 (3–4):310–5. doi: 10.1007/s00217-005-0079-x.
   Web of Science ®Google Scholar
• Rangel, M., M. P. Prado, K. Konno, H. Naoki, J. C. Freitas, and G. M. Machado-Santelli. 2006. Cytoskeleton alterations induced by Geodia corticostylifera depsipeptides in breast cancer cells. Peptides 27 (9):2047–57. doi: 10.1016/j.peptides.2006.04.021.
   PubMed Web of Science ®Google Scholar
• Rashid, M. A., K. R. Gustafson, L. K. Cartner, N. Shigematsu, L. K. Pannell, and M. R. Boyd. 2001. Microspinosamide, a New HIV-inhibitory cyclic depsipeptide from the marine sponge sidonops m icrospinosa. Journal of Natural Products 64 (1):117–21. doi: 10.1021/np0002379.
   PubMed Web of Science ®Google Scholar
• Raymond, E., N. Ady-Vago, E. Baudin, V. Ribrag, S. Faivre, F. Lecot, T. Wright, L. Lazaro, C. Guzman, and J. Jimeno. 2000. A phase I and pharmacokinetic study of aplidine (APL) given as a 24-hour continuous infusion every other week (q2w) in patients (pts) with solid tumor (ST) and lymphoma (NHL). Proceedings 11th NCI-EORTC-AACR Symposium 2000. Amsterdam. 7–10 November, p. 86.
   Google Scholar
• Rho, S. J., J.-S. Lee, Y. I. Chung, Y.-W. Kim, and H. G. Lee. 2009. Purification and identification of an angiotensin I-converting enzyme inhibitory peptide from fermented soybean extract. Process Biochemistry 44 (4):490–3. doi: 10.1016/j.procbio.2008.12.017.
   Web of Science ®Google Scholar
• Ribrag, V., D. Caballero, C. Ferme, E. Zucca, R. Arranz, J. Briones, C. Gisselbrecht, G. Salles, A. M. Gianni, H. Gomez, et al. 2013. Multicenter phase II study of plitidepsin in patients with relapsed/refractory non-Hodgkin’s lymphoma. haematologica 98 (3):357–63. doi: 10.3324/haematol.2012.069757.
   PubMed Web of Science ®Google Scholar
• Richard, N. L., L. F. Pivarnik, P. C. Ellis, and C. M. Lee. 2011. Impact of quality parameters on the recovery of putrescine and cadaverine in fish using methanol-hydrochloric acid solvent extraction. Journal of AOAC International 94 (4):1177–88.
   PubMed Web of Science ®Google Scholar
• Rudi, A., L. Chill, M. Aknin, and Y. Kashman. 2003. Didmolamide A and B, two new cyclic hexapeptides from the marine ascidian Didemnum m olle. Journal of Natural Products 66 (4):575–7. doi: 10.1021/np020531w.
   PubMed Web of Science ®Google Scholar
• Ryu, G., S. Matsunaga, and N. Fusetani. 1994a. Discodermin E, a cytotoxic and antimicrobial tetradecapeptide, from the marine sponge Discodermia kiiensis. Tetrahedron Letters 35 (44):8251–4. doi: 10.1016/0040-4039(94)88295-9.
   Web of Science ®Google Scholar
• Ryu, G., S. Matsunaga, and N. Fusetani. 1994b. Discodermins FH, cytotoxic and antimicrobial tetradecapeptides from the marine sponge Discodermia kiiensis: Structure revision of discodermins AD. Tetrahedron 50 (47):13409–16. doi: 10.1016/S0040-4020(01)89347-9.
   Web of Science ®Google Scholar
• Sagar, S., M. Kaur, and K. P. Minneman. 2010. Antiviral lead compounds from marine sponges. Marine Drugs 8 (10):2619–38. doi: 10.3390/md8102619.
   PubMed Web of Science ®Google Scholar
• Saidi, S., M.-P. Belleville, A. Deratani, and R. Ben Amar. 2016. Production of interesting peptide fractions by enzymatic hydrolysis of tuna dark muscle by-product using alcalase. Journal of Aquatic Food Product Technology 25 (2):251–64. doi: 10.1080/10498850.2013.844753.
   Web of Science ®Google Scholar
• Sakai, R., J. G. Stroh, D. W. Sullins, and K. L. Rinehart. 1995. Seven new didemnins from the marine tunicate Trididemnum solidum. Journal of the American Chemical Society 117 (13):3734–48. doi: 10.1021/ja00118a010.
   Web of Science ®Google Scholar
• Salazar, R., R. J. Jones, A. Oaknin, D. Crawford, C. Cuadra, C. Hopkins, M. Gil, C. Coronado, A. Soto-Matos, M. Cullell-Young, et al. 2012. A phase I and pharmacokinetic study of elisidepsin (PM02734) in patients with advanced solid tumors. Cancer Chemotherapy and Pharmacology 70 (5):673–81. doi: 10.1007/s00280-012-1951-6.
   PubMed Web of Science ®Google Scholar
• Sánchez, A., and A. Vázquez. 2017. Bioactive peptides: A review. Food Quality and Safety 1 (1):29–46. doi: 10.1093/fqsafe/fyx006.
   Web of Science ®Google Scholar
• Sarmadi, B. H., and A. Ismail. 2010. Antioxidative peptides from food proteins: A review. Peptides 31 (10):1949–56. doi: 10.1016/j.peptides.2010.06.020.
   PubMed Web of Science ®Google Scholar
• Sasaki, H., T. Teruya, H. Fukazawa, and K. Suenaga. 2011. Revised structure and structure–activity relationship of bisebromoamide and structure of norbisebromoamide from the marine cyanobacterium Lyngbya sp. Tetrahedron 67 (5):990–4. doi: 10.1016/j.tet.2010.11.106.
   Web of Science ®Google Scholar
• Schmidt, E. W., C. Raventos-Suarez, M. Bifano, A. T. Menendez, C. R. Fairchild, and D. J. Faulkner. 2004. Scleritodermin A, a cytotoxic cyclic peptide from the lithistid sponge Scleritoderma nodosum. Journal of Natural Products 67 (3):475–8. doi: 10.1021/np034035z.
   PubMed Web of Science ®Google Scholar
• Sekar, S., and M. Chandramohan. 2008. Phycobiliproteins as a commodity: Trends in applied research, patents and commercialization. Journal of Applied Phycology 20 (2):113–36. doi: 10.1007/s10811-007-9188-1.
   Web of Science ®Google Scholar
• Senevirathne, M., and S.-K. Kim. 2012. Development of bioactive peptides from fish proteins and their health promoting ability. Advances in Food and Nutrition Research 65:235–48. doi: 10.1016/B978-0-12-416003-3.00015-9.
   PubMedGoogle Scholar
• Serova, M., A. de Gramont, I. Bieche, M. E. Riveiro, C. M. Galmarini, M. Aracil, J. Jimeno, S. Faivre, and E. Raymond. 2013. Predictive factors of sensitivity to elisidepsin, a novel Kahalalide F-derived marine compound. Marine Drugs 11 (3):944–59. doi: 10.3390/md11030944.
   PubMed Web of Science ®Google Scholar
• Shaheen, F., M. A. Ziaee, S. A. Ali, S. U. Simjee, A. Ahmed, and M. I. Choudhary. 2016. The first solid-phase synthesis and structural studies on Phakellistatin 15. Records of Natural Products 10:397–406.
   Web of Science ®Google Scholar
• Shukla, S. 2016. Therapeutic importance of peptides from marine source: A mini review. Indian Journal of Geo-Marine Sciences 45 (11):1422–1431.
   Web of Science ®Google Scholar
• Siro, I., E. Kápolna, B. Kápolna, and A. Lugasi. 2008. Functional food. Product development, marketing and consumer acceptance—A review. Appetite 51 (3):456–67. doi: 10.1016/j.appet.2008.05.060.
   PubMed Web of Science ®Google Scholar
• Sone, H., T. Kondo, M. Kiryu, H. Ishiwata, M. Ojika, and K. Yamada. 1995. Dolabellin, a cytotoxic bisthiazole metabolite from the sea hare Dolabella auricularia: Structural determination and synthesis. The Journal of Organic Chemistry 60 (15):4774–81. doi: 10.1021/jo00120a021.
   Web of Science ®Google Scholar
• Song, R., R. Wei, B. Zhang, and D. Wang. 2012. Optimization of the antibacterial activity of half-fin anchovy (Setipinna taty) hydrolysates. Food and Bioprocess Technology 5 (5):1979–89. doi: 10.1007/s11947-010-0505-3.
   Web of Science ®Google Scholar
• Stensvåg, K., T. Haug, S. V. Sperstad, Ø. Rekdal, B. Indrevoll, and O. B. Styrvold. 2008. Arasin 1, a proline-arginine-rich antimicrobial peptide isolated from the spider crab, Hyas araneus. Developmental and Comparative Immunology 32 (3):275–85. doi: 10.1016/j.dci.2007.06.002.
   PubMed Web of Science ®Google Scholar
• Sugahara, T., Y. Ohama, A. Fukuda, M. Hayashi, A. Kawakubo, and K. Kato. 2001. The cytotoxic effect of Eucheuma serra agglutinin (ESA) on cancer cells and its application to molecular probe for drug delivery system using lipid vesicles. Cytotechnology 36 (1–3):93–9.
   PubMed Web of Science ®Google Scholar
• Swersey, J. C., C. M. Ireland, L. M. Cornell, and R. W. Peterson. 1994. Eusynstyelamide, a highly modified dimer peptide from the ascidian Eusynstyela misakiensis. Journal of Natural Products 57 (6):842–5. doi: 10.1021/np50108a027.
   PubMed Web of Science ®Google Scholar
• Talpir, R., Y. Benayahu, Y. Kashman, L. Pannell, and M. Schleyer. 1994. Hemiasterlin and geodiamolide TA; two new cytotoxic peptides from the marine sponge Hemiasterella minor (Kirkpatrick). Tetrahedron Letters 35 (25):4453–6. doi: 10.1016/S0040-4039(00)73382-X.
   Web of Science ®Google Scholar
• Taylor, S. A., D. J. Giroux, K. A. Jaeckle, T. J. Panella, S. R. Dakhil, and S. C. Schold. 1998. Phase II study of didemnin B in central nervous system tumors: A southwest oncology group study. Investigational New Drugs 16 (4):331–2. doi: 10.1023/A:1006273214056.
   PubMed Web of Science ®Google Scholar
• Teixidó, C., E. Arguelaguet, B. Pons, M. Aracil, J. Jimeno, R. Somoza, R. Marés, S. Ramón y Cajal, and J. Hernández-Losa. 2012. ErbB3 expression predicts sensitivity to elisidepsin treatment: In vitro synergism with cisplatin, paclitaxel and gemcitabine in lung, breast and colon cancer cell lines. International Journal of Oncology 41 (1):317–24. doi: 10.3892/ijo.2012.1425.
   PubMed Web of Science ®Google Scholar
• Teixido, C., Mares, R. Aracil, M. Cajal, y S. R. Hernandez-Losa. and J. 2013. Epithelial-mesenchymal transition markers and HER3 expression are predictors of elisidepsin treatment response in breast and pancreatic cancer cell lines. PLoS One 8 (1):e53645. doi: 10.1371/journal.pone.0053645.
   PubMed Web of Science ®Google Scholar
• Teruya, T., H. Sasaki, H. Fukazawa, and K. Suenaga. 2009. Bisebromoamide, a potent cytotoxic peptide from the marine cyanobacterium Lyngbya sp.: isolation, stereostructure, and biological activity. Organic Letters 11 (21):5062–5. doi: 10.1021/ol9020546.
   PubMed Web of Science ®Google Scholar
• Tincu, J. A., and S. W. Taylor. 2004. Antimicrobial peptides from marine invertebrates. Antimicrobial Agents and Chemotherapy 48 (10):3645–54. doi: 10.1128/AAC.48.10.3645-3654.2004.
   PubMed Web of Science ®Google Scholar
• Tinto, W. F., A. J. Lough, S. McLean, W. F. Reynolds, M. Yu, and W. R. Chan. 1998. Geodiamolides H and I, further cyclodepsipeptides from the marine sponge Geodia sp. Tetrahedron 54 (18):4451–8. doi: 10.1016/S0040-4020(98)00157-4.
   Web of Science ®Google Scholar
• Toske, S. G., and W. Fenical. 1995. Cyclodidemnamide: A new cyclic heptapeptide from the marine ascidian Didemnum molle. Tetrahedron Letters 36 (46):8355–8. doi: 10.1016/0040-4039(95)01806-S.
   Web of Science ®Google Scholar
• Tran, T. D., N. B. Pham, G. A. Fechner, J. N. Hooper, and R. J. Quinn. 2014. Potent cytotoxic peptides from the Australian marine sponge Pipestela candelabra. Marine Drugs 12:3399–415. doi: 10.3390/md12063399.
   PubMed Web of Science ®Google Scholar
• Tran, T. D., N. B. Pham, G. Fechner, D. Zencak, H. T. Vu, J. N. Hooper, and R. J. Quinn. 2012. Cytotoxic cyclic depsipeptides from the Australian marine sponge Neamphius huxleyi. Journal of Natural Products 75:2200–8. doi: 10.1021/np3006474.
   PubMed Web of Science ®Google Scholar
• Ucak, I., M. Afreen, D. Montesano, C. Carrillo, I. Tomasevic, J. Simal-Gandara, and F. J. Barba. 2021. Functional and bioactive properties of peptides derived from marine side streams. Marine Drugs 19 (2):71. doi: 10.3390/md19020071.
   PubMed Web of Science ®Google Scholar
• Uzair, B., S. Tabassum, M. Rasheed, and S. F. Rehman. 2012. Exploring marine cyanobacteria for lead compounds of pharmaceutical importance. The Scientific World Journal 2012:1–10. doi: 10.1100/2012/179782.
   Google Scholar
• Vasko, R. C., R. A. Rodriguez, C. N. Cunningham, V. C. Ardi, D. A. Agard, and S. R. McAlpine. 2010. Mechanistic studies of Sansalvamide A-amide: An allosteric modulator of Hsp90. ACS Medicinal Chemistry Letters 1:4–8. doi: 10.1021/ml900003t.
   PubMed Web of Science ®Google Scholar
• Vera, M. D., and M. M. Joullié. 2002. Natural products as probes of cell biology: 20 years of didemnin research. Medicinal Research Reviews 22:102–45. doi: 10.1002/med.10003.
   PubMed Web of Science ®Google Scholar
• Vervoort, H., W. Fenical, and R. d. A. Epifanio. 2000. Tamandarins A and B: New cytotoxic depsipeptides from a Brazilian ascidian of the family Didemnidae. The Journal of Organic Chemistry 65:782–92. doi: 10.1021/jo991425a.
   PubMed Web of Science ®Google Scholar
• Vijaykrishnaraj, M., and P. Prabhasankar. 2015. Marine protein hydrolysates: Their present and future perspectives in food chemistry–a review. RSC Advances 5 (44):34864–77. doi: 10.1039/C4RA17205A.
   Web of Science ®Google Scholar
• Wang, J., J. Hu, J. Cui, X. Bai, Y. Du, Y. Miyaguchi, and B. Lin. 2008. Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats. Food Chemistry 111 (2):302–8. doi: 10.1016/j.foodchem.2008.03.059.
   PubMed Web of Science ®Google Scholar
• Wang, X., H. Yu, R. Xing, and P. Li. 2017. Characterization, preparation, and purification of marine bioactive peptides. BioMed Research International 2017:9746720. doi: 10.1155/2017/9746720.
   PubMed Web of Science ®Google Scholar
• Wang, X., Z. Zhang, S. Zhang, F. Yang, M. Yang, J. Zhou, Z. Hu, X. Xu, G. Mao, G. Chen, et al. 2021. Antiaging compounds from marine organisms. Food Research International 143:110313. doi: 10.1016/j.foodres.2021.110313.
   PubMed Web of Science ®Google Scholar
• Wang, L., Y. Zou, and B. Jiang. 2015. Process and kinetic models of hydrochloric acid-extracted collagen from Bighead Carp Scale. 5th International Conference on Information Engineering for Mechanics and Materials, pp. 476–482. doi: 10.2991/icimm-15.2015.90.
   Google Scholar
• Wergedahl, H., B. Liaset, O. A. Gudbrandsen, E. Lied, M. Espe, Z. Muna, S. Mørk, and R. K. Berge. 2004. Fish protein hydrolysate reduces plasma total cholesterol, increases the proportion of HDL cholesterol, and lowers acyl-CoA:cholesterol acyltransferase activity in liver of Zucker rats. The Journal of Nutrition 134 (6):1320–7. doi: 10.1093/jn/134.6.1320.
   PubMed Web of Science ®Google Scholar
• Wesson, K. J., and M. T. Hamann. 1996. Keenamide A, a bioactive cyclic peptide from the marine mollusk Pleurobranchus forskalii. Journal of Natural Products 59 (6):629–31. doi: 10.1021/np960153t.
   PubMed Web of Science ®Google Scholar
• Wijesekara, I., Z.-J. Qian, B. Ryu, D.-H. Ngo, and S.-K. Kim. 2011. Purification and identification of antihypertensive peptides from seaweed pipefish (Syngnathus schlegeli) muscle protein hydrolysate. Food Research International 44 (3):703–7. doi: 10.1016/j.foodres.2010.12.022.
   Web of Science ®Google Scholar
• Williams, P. G., W. Y. Yoshida, R. E. Moore, and V. J. Paul. 2002. Isolation and structure determination of obyanamide, a novel cytotoxic cyclic depsipeptide from the marine cyanobacterium Lyngbya confervoides. Journal of Natural Products 65 (1):29–31. doi: 10.1021/np0102253.
   PubMed Web of Science ®Google Scholar
• Wipf, P., P. C. Fritch, S. J. Geib, and A. M. Sefler. 1998. Conformational studies and structure − activity analysis of lissoclinamide 7 and related cyclopeptide alkaloids. Journal of the American Chemical Society 120 (17):4105–12. doi: 10.1021/ja973580h.
   Web of Science ®Google Scholar
• Wipf, P., C. P. Miller, S. Venkatraman, and P. C. Fritch. 1995. Thiolysis of oxazolines: A new, selective method for the direct conversion of peptide oxazolines into thiazolines. Tetrahedron Letters 36 (36):6395–8. doi: 10.1016/0040-4039(95)01322-9.
   Web of Science ®Google Scholar
• Wrasidlo, W., A. Mielgo, V. A. Torres, S. Barbero, K. Stoletov, T. L. Suyama, R. L. Klemke, W. H. Gerwick, D. A. Carson, and D. G. Stupack. 2008. The marine lipopeptide somocystinamide A triggers apoptosis via caspase 8. Proceedings of the National Academy of Sciences of the United States of America 105 (7):2313–8. doi: 10.1073/pnas.0712198105.
   PubMed Web of Science ®Google Scholar
• Wu, H.-C., H.-M. Chen, and C.-Y. Shiau. 2003. Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus). Food Research International 36 (9–10):949–57. doi: 10.1016/S0963-9969(03)00104-2.
   Web of Science ®Google Scholar
• Wu, Q.-X., M. S. Crews, M. Draskovic, J. Sohn, T. A. Johnson, K. Tenney, F. A. Valeriote, X.-J. Yao, L. F. Bjeldanes, and P. Crews. 2010. Azonazine, a novel dipeptide from a Hawaiian marine sediment-derived fungus, Aspergillus insulicola. Organic Letters 12 (20):4458–61. doi: 10.1021/ol101396n.
   PubMed Web of Science ®Google Scholar
• Wu, H., H.-L. He, X.-L. Chen, C.-Y. Sun, Y.-Z. Zhang, and B.-C. Zhou. 2008. Purification and identification of novel angiotensin-I-converting enzyme inhibitory peptides from shark meat hydrolysate. Process Biochemistry 43 (4):457–61. doi: 10.1016/j.procbio.2008.01.018.
   Web of Science ®Google Scholar
• Yadav, J., K. Purnima, B. S. Reddy, K. Nagaiah, and A. Ghamdi. 2011. Total synthesis of cryptophycin-24 (arenastatin A) via Prins cyclization. Tetrahedron Letters 52 (50):6709–12. doi: 10.1016/j.tetlet.2011.09.134.
   Web of Science ®Google Scholar
• Yang, L., R.-x. Tan, Q. Wang, W.-y. Huang, and Y.-x. Yin. 2002. Antifungal cyclopeptides from Halobacillus litoralis YS3106 of marine origin. Tetrahedron Letters 43 (37):6545–8. doi: 10.1016/S0040-4039(02)01458-2.
   Web of Science ®Google Scholar
• Younes, A., U. Yasothan, and P. Kirkpatrick. 2012. Brentuximab vedotin. Nature Reviews. Drug Discovery 11 (1):19–20. doi: 10.1038/nrd3629.
   PubMed Web of Science ®Google Scholar
• Yu, Z., G. Lang, I. Kajahn, R. Schmaljohann, and J. F. Imhoff. 2008. Scopularides A and B, cyclodepsipeptides from a marine sponge-derived fungus, Scopulariopsis brevicaulis. Journal of Natural Products 71 (6):1052–4. doi: 10.1021/np070580e.
   PubMed Web of Science ®Google Scholar
• Zampella, A., M. V. D'Auria, L. G. Paloma, A. Casapullo, L. Minale, C. Debitus, and Y. Henin. 1996. Callipeltin A, an anti-HIV cyclic depsipeptide from the New Caledonian Lithistida sponge Callipelta sp. Journal of the American Chemical Society 118 (26):6202–9. doi: 10.1021/ja954287p.
   Web of Science ®Google Scholar
• Zampella, A., V. Sepe, P. Luciano, F. Bellotta, M. C. Monti, M. V. D’Auria, T. Jepsen, S. Petek, M.-T. Adeline, O. LaprévôTe, et al. 2008. Homophymine A, an anti-HIV cyclodepsipeptide from the sponge Homophymia sp. The Journal of Organic Chemistry 73 (14):5319–27. doi: 10.1021/jo800583b.
   PubMed Web of Science ®Google Scholar
• Zeng, M., W. Cui, Y. Zhao, Z. Liu, S. Dong, and Y. Guo. 2008. Antiviral active peptide from oyster. Chinese Journal of Oceanology and Limnology 26 (3):307–12. doi: 10.1007/s00343-008-0307-x.
   Web of Science ®Google Scholar
• Zhan, K.-X., W.-H. Jiao, F. Yang, J. Li, S.-P. Wang, Y.-S. Li, B.-N. Han, and H.-W. Lin. 2014. Reniochalistatins A-E, cyclic peptides from the marine sponge Reniochalina stalagmitis. Journal of Natural Products 77 (12):2678–84. doi: 10.1021/np5006778.
   PubMed Web of Science ®Google Scholar
• Zhang, H.-J., Y.-H. Yi, G.-J. Yang, M.-Y. Hu, G.-D. Cao, F. Yang, and H.-W. Lin. 2010. Proline-containing cyclopeptides from the marine sponge Phakellia fusca. Journal of Natural Products 73 (4):650–5. doi: 10.1021/np9008267.
   PubMed Web of Science ®Google Scholar
• Zhao, Y., B. Li, S. Dong, Z. Liu, X. Zhao, J. Wang, and M. Zeng. 2009. A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate. Peptides 30 (6):1028–33. doi: 10.1016/j.peptides.2009.03.002.
   PubMed Web of Science ®Google Scholar
• Zhao, Y., B. Li, Z. Liu, S. Dong, X. Zhao, and M. Zeng. 2007. Antihypertensive effect and purification of an ACE inhibitory peptide from sea cucumber gelatin hydrolysate. Process Biochemistry 42 (12):1586–91. doi: 10.1016/j.procbio.2007.08.011.
   Web of Science ®Google Scholar
• Zheng, L.-H., Y.-J. Wang, J. Sheng, F. Wang, Y. Zheng, X.-K. Lin, and M. Sun. 2011. Antitumor peptides from marine organisms. Marine Drugs 9 (10):1840–59. doi: 10.3390/md9101840.
   PubMed Web of Science ®Google Scholar
• Zhou, X., C. Wang, and A. Jiang. 2012. Antioxidant peptides isolated from sea cucumber Stichopus Japonicus. European Food Research and Technology 234 (3):441–7. doi: 10.1007/s00217-011-1610-x.
   Web of Science ®Google Scholar
• Ziółkowska, N. E., and A. Wlodawer. 2006. Structural studies of algal lectins with anti-HIV activity. Acta Biochimica Polonica 53 (4):617–26. doi: 10.18388/abp.2006_3290.
   PubMed Web of Science ®Google Scholar