Tachyplesin I and its derivatives: A pharmaco-chemical perspective on their antimicrobial and antitumor potential

References

• Siegel RL, Miller KD, Fuchs HE, et al. Cancer statistics, 2022. CA Cancer J Clin. 2022;72(1):7–33.
   PubMed Web of Science ®Google Scholar
• Zhen X, Stålsby Lundborg C, Sun X, et al. Economic burden of antibiotic resistance in China: a national level estimate for inpatients. Antimicrob Resist Infect Control. 2021;10(1):5.
   PubMed Web of Science ®Google Scholar
• Assaraf YG, Brozovic A, Gonçalves AC, et al. The multi-factorial nature of clinical multidrug resistance in cancer. Drug Resist Updat. 2019;46:100645.
   PubMed Web of Science ®Google Scholar
• Yu LX, Schwabe RF. The gut microbiome and liver cancer: mechanisms and clinical translation. Nat Rev Gastroenterol Hepatol. 2017;14(9):527–539.
   PubMed Web of Science ®Google Scholar
• Garrett WS. Cancer and the microbiota. Science. 2015;348(6230):80–86.
   PubMed Web of Science ®Google Scholar
• Fu A, Yao B, Dong T, et al. Tumor-resident intracellular microbiota promotes metastatic colonization in breast cancer. Cell. 2022;185(8):1356–1372.
   PubMed Web of Science ®Google Scholar
• Geller LT, Barzily-Rokni M, Danino T, et al. Potential role of intratumor bacteria in mediating tumor resistance to the chemotherapeutic drug gemcitabine. Science. 2017;357(6356):1156–1160.
   PubMed Web of Science ®Google Scholar
• Alam A, Levanduski E, Denz P, et al. Fungal mycobiome drives IL-33 secretion and type 2 immunity in pancreatic cancer. Cancer Cell. 2022;40(2):153–167.
   PubMed Web of Science ®Google Scholar
• Murota Y, Jobin C. Bacteria break barrier to promote metastasis. Cancer Cell. 2021;39(5):598–600.
   PubMed Web of Science ®Google Scholar
• Avci FG, Akbulut BS, Ozkirimli E. Membrane active peptides and their biophysical characterization. Biomolecules. 2018;8(3):77.
   PubMed Web of Science ®Google Scholar
• Walls EA, Berkson J, Smith SA. The horseshoe crab, Limulus polyphemus: 200 million years of existence, 100 years of study. Rev Fish Sci. 2010;10(1):39–73.
   Google Scholar
• Marggraf MB, Panteleev PV, Emelianova AA, et al. Cytotoxic potential of the novel horseshoe crab peptide Polyphemusin III. Mar Drugs. 2018;16(12):466.
   PubMed Web of Science ®Google Scholar
• Miyata T, Tokunaga F, Yoneya T, et al. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity. J Biochem. 1989;106(4):663–668.
   PubMed Web of Science ®Google Scholar
• Ohta M, Ito H, Masuda K, et al. Mechanisms of antibacterial action of tachyplesins and polyphemusins, a group of antimicrobial peptides isolated from horseshoe crab hemocytes. Antimicrob Agents Chemother. 1992;36(7):1460–1465.
   PubMed Web of Science ®Google Scholar
• Nakamura T, Furunaka H, Miyata T, et al. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure. J Biol Chem. 1988;263(32):16709–16713.
   PubMed Web of Science ®Google Scholar
• Masuda K, Ohta M, Ito M, et al. Bactericidal action of tachyplesin I against oral streptococci. Oral Microbiol Immunol. 1994;9(2):77–80.
   PubMedGoogle Scholar
• Hong J, Guan W, Jin G, et al. Mechanism of tachyplesin I injury to bacterial membranes and intracellular enzymes,0 determined by laser confocal scanning microscopy and flow cytometry. Microbiol Res. 2015;170:69–77.
   PubMed Web of Science ®Google Scholar
• Liu C, Qi J, Shan B, et al. Tachyplesin causes membrane instability that kills multidrug-resistant bacteria by inhibiting the 3-ketoacyl carrier protein reductase FabG. Front Microbiol. 2018;9:825.
   PubMed Web of Science ®Google Scholar
• Kumar V, Chugh A. Peptide-mediated leishmaniasis management strategy: tachyplesin emerges as an effective anti-leishmanial peptide against Leishmania donovani. Biochim Biophys Acta Biomembr. 2021;1863(8):183629.
   PubMed Web of Science ®Google Scholar
• Murakami T, Niwa M, Tokunaga F, et al. Direct virus inactivation of tachyplesin I and its isopeptides from horseshoe crab hemocytes. Chemotherapy. 1991;37(5):327–334.
   PubMed Web of Science ®Google Scholar
• Xie H, Wei J, Qin Q. Antiviral function of Tachyplesin I against iridovirus and nodavirus. Fish Shellfish Immunol. 2016;58:96–102.
   PubMed Web of Science ®Google Scholar
• Vernen F, Harvey PJ, Dias SA, et al. Characterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties. Int J Mol Sci. 2019;20(17):4184.
   PubMed Web of Science ®Google Scholar
• Ding H, Jin G, Zhang L, et al. Effects of tachyplesin I on human U251 glioma stem cells. Mol Med Rep. 2015;11(4):2953–2958.
   PubMed Web of Science ®Google Scholar
• Ouyang GL, Li Q-F, Peng XX, et al. Effects of tachyplesin on proliferation and differentiation of human hepatocellular carcinoma SMMC-7721 cells. World J Gastroenterol. 2002;8(6):1053–1058.
   PubMed Web of Science ®Google Scholar
• Vernen F, Craik DJ, Lawrence N, et al. Cyclic analogues of horseshoe crab peptide Tachyplesin I with anticancer and cell penetrating properties. ACS Chem Biol. 2019;14(12):2895–2908.
   PubMed Web of Science ®Google Scholar
• Rady I, Siddiqui IA, Rady M, et al. Melittin, a major peptide component of bee venom, and its conjugates in cancer therapy. Cancer Lett. 2017;402:16–31.
   PubMed Web of Science ®Google Scholar
• Wu Y, Lu D, Jiang YX, et al. Stapled wasp venom-derived oncolytic peptides with side chains induce rapid membrane lysis and prolonged immune responses in melanoma. J Med Chem. 2021;64(9):5802–5815.
   PubMed Web of Science ®Google Scholar
• Lu L, Zhang H, Zhou YD, et al. Polymer chimera of stapled oncolytic peptide coupled with anti-PD-L1 peptide boosts immunotherapy of colorectal cancer. Theranostics. 2022;12(7):3456–3473.
   PubMed Web of Science ®Google Scholar
• Ting DSJ, Beuerman RW, Dua HS, et al. Strategies in translating the therapeutic potentials of host defense peptides. Front Immunol. 2020;11:983.
   PubMed Web of Science ®Google Scholar
• Luong HX, Bui HTP, Tung TT. Application of the all-hydrocarbon stapling technique in the design of membrane-active peptides. J Med Chem. 2022;65(4):3026–3045.
   PubMed Web of Science ®Google Scholar
• Tamamura H, Ikoma R, Niwa M, et al. Antimicrobial activity and conformation of tachyplesin I and its analogs. Chem Pharm Bull. 1993;41(5):978–980.
   PubMed Web of Science ®Google Scholar
• Edwards IA, Elliott AG, Kavanagh AM, et al. Structure-activity and -toxicity relationships of the antimicrobial peptide Tachyplesin-1. ACS Infect Dis. 2017;3(12):917–926.
   PubMed Web of Science ®Google Scholar
• Jain A, Yadav BK, Chugh A. Marine antimicrobial peptide tachyplesin as an efficient nanocarrier for macromolecule delivery in plant and mammalian cells. FEBS J. 2015;282(4):732–745.
   PubMed Web of Science ®Google Scholar
• Colgrave ML, Craik DJ. Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: the importance of the cyclic cystine knot. Biochemistry. 2004;43(20):5965–5975.
   PubMed Web of Science ®Google Scholar
• Sharma R, Nisakar D, Shivpuri S, et al. Contrasting effects of cysteine modification on the transfection efficiency of amphipathic peptides. Biomaterials. 2014;35(24):6563–6575.
   PubMed Web of Science ®Google Scholar
• Schmidtchen A, Pasupuleti M, Mörgelin M, et al. Boosting antimicrobial peptides by hydrophobic oligopeptide end tags. J Biol Chem. 2009;284(26):17584–17594.
   PubMed Web of Science ®Google Scholar
• Wang G, Epand RF, Mishra B, et al. Decoding the functional roles of cationic side chains of the major antimicrobial region of human cathelicidin LL-37. Antimicrob Agents Chemother. 2012;56(2):845–856.
   PubMed Web of Science ®Google Scholar
• Panteleev PV, Ovchinnikova TV. Improved strategy for recombinant production and purification of antimicrobial peptide tachyplesin I and its analogs with high cell selectivity. Biotechnol Appl Biochem. 2017;64(1):35–42.
   PubMed Web of Science ®Google Scholar
• Amiss AS, von Pein JB, Webb JR, et al. Modified horseshoe crab peptides target and kill bacteria inside host cells. Cell Mol Life Sci. 2021;79(1):38.
   PubMed Web of Science ®Google Scholar
• Li Y, Cao X, Tian C, et al. Chemical protein synthesis-assisted high-throughput screening strategies for d-peptides in drug discovery. Chin Chem Lett. 2020;31(9):2365–2374.
   Web of Science ®Google Scholar
• Garton M, Nim S, Stone TA, et al. Method to generate highly stable D-amino acid analogs of bioactive helical peptides using a mirror image of the entire PDB. Proc Natl Acad Sci U S A. 2018;115(7):1505–1510.
   PubMed Web of Science ®Google Scholar
• Yu R, Wang J, So LY, et al. Enhanced activity against multidrug-resistant bacteria through coapplication of an analogue of Tachyplesin I and an inhibitor of the QseC/B signaling pathway. J Med Chem. 2020;63(7):3475–3484.
   PubMed Web of Science ®Google Scholar
• Harris JM, Chess RB. Effect of pegylation on pharmaceuticals. Nat Rev Drug Discov. 2003;2(3):214–221.
   PubMed Web of Science ®Google Scholar
• Imura Y, Nishida M, Ogawa Y, et al. Action mechanism of tachyplesin I and effects of PEGylation. Biochim Biophys Acta. 2007;1768(5):1160–1169.
   PubMed Web of Science ®Google Scholar
• Kuzmin DV, Emelianova AA, Kalashnikova MB, et al. Effect of N- and C-terminal modifications on cytotoxic properties of antimicrobial peptide Tachyplesin I. Bull Exp Biol Med. 2017;162(6):754–757.
   PubMed Web of Science ®Google Scholar
• Morrison C. Constrained peptides’ time to shine? Nat Rev Drug Discov. 2018;17(8):531–533.
   PubMed Web of Science ®Google Scholar
• Chow HY, Zhang Y, Matheson E, et al. Ligation technologies for the synthesis of cyclic peptides. Chem Rev. 2019;119(17):9971–10001.
   PubMed Web of Science ®Google Scholar
• Usmani SS, Bedi G, Samuel JS, et al. THPdb: database of FDA-approved peptide and protein therapeutics. PLoS One. 2017;12(7):e0181748.
   PubMed Web of Science ®Google Scholar
• Zhang H, Chen S. Cyclic peptide drugs approved in the last two decades (2001-2021). RSC Chem Biol. 2022;3(1):18–31.
   PubMedGoogle Scholar
• Patil NA, Tailhades J, Hughes RA, et al. Cellular disulfide bond formation in bioactive peptides and proteins. Int J Mol Sci. 2015;16(1):1791–1805.
   PubMed Web of Science ®Google Scholar
• Gamcsik MP, Kasibhatla MS, Teeter SD, et al. Glutathione levels in human tumors. Biomarkers. 2012;17(8):671–691.
   PubMed Web of Science ®Google Scholar
• Qi YK, Qu Q, Bierer D, et al. A Diaminodiacid (DADA) strategy for the development of disulfide surrogate peptides. Chem Asian J. 2020;15(18):2793–2802.
   PubMed Web of Science ®Google Scholar
• Zhao R, Shi P, Chen J, et al. Chemical synthesis and biological activity of peptides incorporating an ether bridge as a surrogate for a disulfide bond. Chem Sci. 2020;11(30):7927–7932.
   PubMed Web of Science ®Google Scholar
• Cui HK, Guo Y, He Y, et al. Diaminodiacid-based solid-phase synthesis of peptide disulfide bond mimics. Angew Chem Int Ed In. 2013;52(36): 9558–9562
   Google Scholar
• Holland-Nell K, Meldal M. Maintaining biological activity by using triazoles as disulfide bond mimetics. Angew Chem Int Ed. 2011;50(22):5204–5206.
   PubMed Web of Science ®Google Scholar
• Marc MA, Kincses A, Rácz B, et al. Antimicrobial, anticancer and multidrug-resistant reversing activity of novel oxygen-, sulfur- and selenoflavones and bioisosteric analogues. Pharmaceuticals. 2020;13(12):453.
   Web of Science ®Google Scholar
• Schneider T, Baldauf A, Ba LA, et al. Selective antimicrobial activity associated with sulfur nanoparticles. J Biomed Nanotechnol. 2011;7(3):395–405.
   PubMed Web of Science ®Google Scholar
• Fjell CD, Hiss JA, Hancock REW, et al. Designing antimicrobial peptides: form follows function. Nat Rev Drug Discov. 2011;11(1):37–51.
   PubMed Web of Science ®Google Scholar
• Spohn R, Daruka L, Lázár V, et al. Integrated evolutionary analysis reveals antimicrobial peptides with limited resistance. Nat Commun. 2019;10(1):4538.
   PubMedGoogle Scholar
• Jenssen H, Hamill P, Hancock REW. Peptide antimicrobial agents. Clin Microbiol Rev. 2006;19(3):491–511.
   PubMed Web of Science ®Google Scholar
• Bevers EM, Comfurius P, Zwaal RF. Regulatory mechanisms in maintenance and modulation of transmembrane lipid asymmetry: pathophysiological implications. Lupus. 1996;5(5):480–487.
   PubMed Web of Science ®Google Scholar
• Silhavy TJ, Kahne D, Walker S. The bacterial cell envelope. Cold Spring Harb Perspect Biol. 2010;2(5):a000414.
   PubMed Web of Science ®Google Scholar
• Zwaal RFA, Comfurius P, Bevers EM. Surface exposure of phosphatidylserine in pathological cells. Cell Mol Life Sci. 2005;62(9):971–988.
   PubMed Web of Science ®Google Scholar
• Buri MV, Sperandio LP, de Souza KFS, et al. Endocytosis and the participation of glycosaminoglycans are important to the mechanism of cell death induced by ß-hairpin antimicrobial peptides. ACS Appl Bio Mater. 2021;4(8):6488–6501.
   PubMedGoogle Scholar
• Walrant A, Bauzá A, Girardet C, et al. Ionpair-p interactions favor cell penetration of arginine/tryptophan-rich cell-penetrating peptides. Biochim Biophys Acta Biomembr. 2020;1862(2):183098.
   PubMed Web of Science ®Google Scholar
• Bobone S, Stella L. (2019). Selectivity of Antimicrobial Peptides: A Complex Interplay of Multiple Equilibria. Adv Exp Med Biol, 1117 175–214. 10.1007/978-981-13-3588-4_11
   PubMed Web of Science ®Google Scholar
• Baxter AA, Lay FT, Poon IKH, et al. Tumor cell membrane-targeting cationic antimicrobial peptides: novel insights into mechanisms of action and therapeutic prospects. Cell Mol Life Sci. 2017;74(20):3809–3825.
   PubMed Web of Science ®Google Scholar
• Li J, Lu X, Ma W, et al. Cholesterols work as a molecular regulator of the antimicrobial peptide-membrane interactions. Front Mol.Biosci. 2021;8. 638988.
   PubMed Web of Science ®Google Scholar
• Buri M V, Torquato H F, Barros C Castilho, Ide J S, Miranda A, Paredes-Gamero E J. (2017). Comparison of Cytotoxic Activity in Leukemic Lineages Reveals Important Features of β-Hairpin Antimicrobial Peptides. J Cell Biochem, 118(7), 1764–1773. 10.1002/jcb.25844
   PubMed Web of Science ®Google Scholar
• Ramamoorthy A, Thennarasu S, Tan A, et al. Deletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective binding. Biochemistry. 2006;45(20):6529–6540.
   PubMed Web of Science ®Google Scholar
• Rao A G. (1999). Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds. Arch Biochem Biophys, 361(1), 127–34. 10.1006/abbi.1998.0962
   PubMed Web of Science ®Google Scholar
• Shi J, So L, Chen F, Liang J, Chow H, Wong K, Wan S, Jiang T, Yu R. (2018). Influences of disulfide connectivity on structure and antimicrobial activity of tachyplesin I. J Pept Sci, 24(6), e3087 10.1002/psc.3087
   PubMed Web of Science ®Google Scholar
• Kwun M Seok, Lee D Gun. (2021). Apoptosis-like death-inducing property of tachyplesin I in Escherichia coli. J Basic Microbiol, 61(9), 795–807. 10.1002/jobm.202100133
   PubMed Web of Science ®Google Scholar
• Li W, Li Y, Sun P, Zhang N, Zhao Y, Qin S, Zhao Y. (2020). Antimicrobial peptide-modified silver nanoparticles for enhancing the antibacterial efficacy. RSC Adv, 10(64), 38746–38754. 10.1039/d0ra05640e
   PubMed Web of Science ®Google Scholar
• Safronova V N, Panteleev P V, Sukhanov S V, Toropygin I Y, Bolosov I A, Ovchinnikova T V. (2022). Mechanism of Action and Therapeutic Potential of the β-Hairpin Antimicrobial Peptide Capitellacin from the Marine Polychaeta Capitella teleta. Mar Drugs, 20(3),– 10.3390/md20030167
   Web of Science ®Google Scholar
• Panteleev P V, Tsarev A V, Safronova V N, Reznikova O V, Bolosov I A, Sychev S V, Shenkarev Z O, Ovchinnikova T V. (2020). Structure Elucidation and Functional Studies of a Novel β-hairpin Antimicrobial Peptide from the Marine Polychaeta Capitella teleta. Mar Drugs, 18(12),– 10.3390/md18120620
   Web of Science ®Google Scholar
• Miao F, Tai Z, Wang Y, Zhu Q, Fang J Kar-Hei, Hu M. (2022). Tachyplesin I Analogue Peptide as an Effective Antimicrobial Agent against Candida albicans-Staphylococcus aureus Poly-Biofilm Formation and Mixed Infection. ACS Infect Dis, 8(9), 1839–1850. 10.1021/acsinfecdis.2c00080
   PubMed Web of Science ®Google Scholar
• Priya A, Aditya A, Budagavi D Poornima, Chugh A. (2022). Tachyplesin and CyLoP-1 as efficient anti-mycobacterial peptides: A novel finding. Biochim Biophys Acta Biomembr, 1864(7), 183895 10.1016/j.bbamem.2022.183895
   PubMed Web of Science ®Google Scholar
• Yonezawa A, Kuwahara J, Fujii N, Sugiura Y. (1992). Binding of tachyplesin I to DNA revealed by footprinting analysis: significant contribution of secondary structure to DNA binding and implication for biological action. Biochemistry, 31(11), 2998–3004. 10.1021/bi00126a022
   PubMed Web of Science ®Google Scholar
• Miyazaki Y, Aoki M, Yano Y, Matsuzaki K. (2012). Interaction of antimicrobial peptide magainin 2 with gangliosides as a target for human cell binding. Biochemistry, 51(51), 10229–35. 10.1021/bi301470h
   PubMed Web of Science ®Google Scholar
• Matsuzaki K, Yoneyama S, Fujii N, Miyajima K, Yamada K, Kirino Y, Anzai K. (1997). Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, tachyplesin I, and its linear analog. Biochemistry, 36(32), 9799–806. 10.1021/bi970588v
   PubMed Web of Science ®Google Scholar
• Matsuzaki K, Nakayama M, Fukui M, Otaka A, Funakoshi S, Fujii N, Bessho K, Miyajima K. (1993). Role of disulfide linkages in tachyplesin-lipid interactions. Biochemistry, 32(43), 11704–10. 10.1021/bi00094a029
   PubMed Web of Science ®Google Scholar
• Laederach A, Andreotti A H, Fulton D Bruce. (2002). Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives. Biochemistry, 41(41), 12359–68. 10.1021/bi026185z
   PubMed Web of Science ®Google Scholar
• Pang Z, Raudonis R, Glick B R, Lin T, Cheng Z. (2019). Antibiotic resistance in Pseudomonas aeruginosa: mechanisms and alternative therapeutic strategies. Biotechnol Adv, 37(1), 177–192. 10.1016/j.biotechadv.2018.11.013
   PubMed Web of Science ®Google Scholar
• Davies D. (2003). Understanding biofilm resistance to antibacterial agents. Nat Rev Drug Discov, 2(2), 114–22. 10.1038/nrd1008
   PubMed Web of Science ®Google Scholar
• Rather M Ahmad, Gupta K, Mandal M. (2021). Microbial biofilm: formation, architecture, antibiotic resistance, and control strategies. Braz J Microbiol, 52(4), 1701–1718. 10.1007/s42770-021-00624-x
   PubMed Web of Science ®Google Scholar
• Dwyer D J, Camacho D M, Kohanski M A, Callura J M, Collins J J. (2012). Antibiotic-induced bacterial cell death exhibits physiological and biochemical hallmarks of apoptosis. Mol Cell, 46(5), 561–72. 10.1016/j.molcel.2012.04.027
   PubMed Web of Science ®Google Scholar
• Bayles K W. (2014). Bacterial programmed cell death: making sense of a paradox. Nat Rev Microbiol, 12(1), 63–9. 10.1038/nrmicro3136
   PubMed Web of Science ®Google Scholar
• Benfield A H et al . (2021). Cyclic gomesin, a stable redesigned spider peptide able to enter cancer cells. Biochim Biophys Acta Biomembr, 1863(1), 183480 10.1016/j.bbamem.2020.183480
   PubMed Web of Science ®Google Scholar
• Niu M, Chai S, You X, Wang W, Qin C, Gong Q, Zhang T, Wan P. (2015). Expression of porcine protegrin-1 in Pichia pastoris and its anticancer activity in vitro. Exp Ther Med, 9(3), 1075–1079. 10.3892/etm.2015.2202
   PubMed Web of Science ®Google Scholar
• Kuzmin D V, Emel'yanova A A, Kalashnikova M B, Panteleev P V, Ovchinnikova T V. (2018). In Vitro Study of Antitumor Effect of Antimicrobial Peptide Tachyplesin I in Combination with Cisplatin. Bull Exp Biol Med, 165(2), 220–224. 10.1007/s10517-018-4134-6
   PubMed Web of Science ®Google Scholar
• Li X, Dai J, Tang Y, Li L, Jin G. (2017). Quantitative Proteomic Profiling of Tachyplesin I Targets in U251 Gliomaspheres. Mar Drugs, 15(1),– 10.3390/md15010020
   Web of Science ®Google Scholar
• Zhang H, Wu J, Zhang H, Zhu Q. (2006). Efflux of potassium ion is an important reason of HL-60 cells apoptosis induced by tachyplesin. Acta Pharmacol Sin, 27(10), 1367–74. 10.1111/j.1745-7254.2006.00377.x
   PubMed Web of Science ®Google Scholar
• Wu J et al . (2021). Tachyplesin induces apoptosis in non-small cell lung cancer cells and enhances the chemosensitivity of A549/DDP cells to cisplatin by activating Fas and necroptosis pathway. Chem Biol Drug Des, 97(4), 809–820. 10.1111/cbdd.13810
   PubMed Web of Science ®Google Scholar
• Paredes-Gamero E J, Martins M N, Cappabianco F A, Ide J S, Miranda A. (2012). Characterization of dual effects induced by antimicrobial peptides: regulated cell death or membrane disruption. Biochim Biophys Acta, 1820(7), 1062–72. 10.1016/j.bbagen.2012.02.015
   PubMed Web of Science ®Google Scholar
• Kuzmin D V, Emelianova A A, Kalashnikova M B, Panteleev P V, Balandin S V, Serebrovskaya E O, Belogurova-Ovchinnikova O Y, Ovchinnikova T V. (2018). Comparative in vitro study on cytotoxicity of recombinant β-hairpin peptides. Chem Biol Drug Des, 91(1), 294–303. 10.1111/cbdd.13081
   PubMed Web of Science ®Google Scholar
• Li Q, Ou-Yang G, Peng X, Hong S. (2003). Effects of tachyplesin on the regulation of cell cycle in human hepatocarcinoma SMMC-7721 cells. World J Gastroenterol, 9(3), 454–8. 10.3748/wjg.v9.i3.454
   PubMed Web of Science ®Google Scholar
• Shi S, Wang Y, Liang Y, Li Q. (2006). Effects of tachyplesin and n-sodium butyrate on proliferation and gene expression of human gastric adenocarcinoma cell line BGC-823. World J Gastroenterol, 12(11), 1694–8. 10.3748/wjg.v12.i11.1694
   PubMed Web of Science ®Google Scholar
• Chen J, Xu X, Underhill C B, Yang S, Wang L, Chen Y, Hong S, Creswell K, Zhang L. (2005). Tachyplesin activates the classic complement pathway to kill tumor cells. Cancer Res, 65(11), 4614–22. 10.1158/0008-5472.CAN-04-2253
   PubMed Web of Science ®Google Scholar
• Ghisaidoobe A B, Chung S J. (2014). Intrinsic tryptophan fluorescence in the detection and analysis of proteins: a focus on Förster resonance energy transfer techniques. Int J Mol Sci, 15(12), 22518–38. 10.3390/ijms151222518
   PubMed Web of Science ®Google Scholar
• Partida-Hanon A, Maestro-López M, Vitale S, Turrà D, Di Pietro A, Martínez-Del-Pozo Á, Bruix M. (2020). Structure of Fungal α Mating Pheromone in Membrane Mimetics Suggests a Possible Role for Regulation at the Water-Membrane Interface. Front Microbiol, 11 1090 10.3389/fmicb.2020.01090
   PubMed Web of Science ®Google Scholar
• Barbosa S C, Cilli E M, Dias L G, Fuzo C A, Degrève L, Stabeli R G, Itri R, Ciancaglini P. (2015). Interaction of cyclic and linear Labaditin peptides with anionic and zwitterionic micelles. J Colloid Interface Sci, 438 39–46. 10.1016/j.jcis.2014.09.059
   PubMed Web of Science ®Google Scholar
• Bonucci A, Caldaroni E, Balducci E, Pogni R. (2015). A Spectroscopic Study of the Aggregation State of the Human Antimicrobial Peptide LL-37 in Bacterial versus Host Cell Model Membranes. Biochemistry, 54(45), 6760–8. 10.1021/acs.biochem.5b00813
   PubMed Web of Science ®Google Scholar
• Schapira A H. (2012). Mitochondrial diseases. Lancet, 379(9828), 1825–34. 10.1016/S0140-6736(11)61305-6
   PubMed Web of Science ®Google Scholar
• Shoshan-Barmatz V, De Pinto V, Zweckstetter M, Raviv Z, Keinan N, Arbel N. (2010). VDAC, a multi-functional mitochondrial protein regulating cell life and death. Mol Aspects Med, 31(3), 227–85. 10.1016/j.mam.2010.03.002
   PubMed Web of Science ®Google Scholar
• Chen Y, Xu X, Hong S, Chen J, Liu N, Underhill C B, Creswell K, Zhang L. (2001). RGD-Tachyplesin inhibits tumor growth. Cancer Res, 61(6), 2434–8.
   PubMed Web of Science ®Google Scholar
• Bortner C D, Hughes F M, Cidlowski J A. (1997). A primary role for K+ and Na+ efflux in the activation of apoptosis. J Biol Chem, 272(51), 32436–42. 10.1074/jbc.272.51.32436
   PubMed Web of Science ®Google Scholar
• Su Z, Yang Z, Xu Y, Chen Y, Yu Q. (2015). Apoptosis, autophagy, necroptosis, and cancer metastasis. Mol Cancer, 14 48 10.1186/s12943-015-0321-5
   PubMed Web of Science ®Google Scholar
• Agostinho M, Santos V, Ferreira F, Costa R, Cardoso J, Pinheiro I, Rino J, Jaffray E, Hay R T, Ferreira J. (2008). Conjugation of human topoisomerase 2 alpha with small ubiquitin-like modifiers 2/3 in response to topoisomerase inhibitors: cell cycle stage and chromosome domain specificity. Cancer Res, 68(7), 2409–18. 10.1158/0008-5472.CAN-07-2092
   PubMed Web of Science ®Google Scholar
• Ganapathy-Kanniappan S, Geschwind J H. (2013). Tumor glycolysis as a target for cancer therapy: progress and prospects. Mol Cancer, 12 152 10.1186/1476-4598-12-152
   PubMed Web of Science ®Google Scholar
• Fehrenbacher N, Jäättelä M. (2005). Lysosomes as targets for cancer therapy. Cancer Res, 65(8), 2993–5. 10.1158/0008-5472.CAN-05-0476
   PubMed Web of Science ®Google Scholar
• Massagué J. (2004). G1 cell-cycle control and cancer. Nature, 432(7015), 298–306. 10.1038/nature03094
   PubMed Web of Science ®Google Scholar
• Otto T, Sicinski P. (2017). Cell cycle proteins as promising targets in cancer therapy. Nat Rev Cancer, 17(2), 93–115. 10.1038/nrc.2016.138
   PubMed Web of Science ®Google Scholar
• Yang J Dong, Heimbach J K. (2020). New advances in the diagnosis and management of hepatocellular carcinoma. BMJ, 371 m3544 10.1136/bmj.m3544
   PubMed Web of Science ®Google Scholar
• De Grandi A et al . (2020). Highly Elevated Plasma γ-Glutamyltransferase Elevations: A Trait Caused by γ-Glutamyltransferase 1 Transmembrane Mutations. Hepatology, 71(3), 1124–1127. 10.1002/hep.30944
   PubMed Web of Science ®Google Scholar
• Witko-Sarsat V, Ohayon D. (2016). Proliferating cell nuclear antigen in neutrophil fate. Immunol Rev, 273(1), 344–56. 10.1111/imr.12449
   PubMed Web of Science ®Google Scholar
• El-Deiry W S. (2016). p21(WAF1) Mediates Cell-Cycle Inhibition, Relevant to Cancer Suppression and Therapy. Cancer Res, 76(18), 5189–91. 10.1158/0008-5472.CAN-16-2055
   PubMed Web of Science ®Google Scholar
• Thompson E B. (1998). The many roles of c-Myc in apoptosis. Annu Rev Physiol, 60 575–600. 10.1146/annurev.physiol.60.1.575
   PubMed Web of Science ®Google Scholar
• Bai X, Ni J, Beretov J, Graham P, Li Y. (2018). Cancer stem cell in breast cancer therapeutic resistance. Cancer Treat Rev, 69 152–163. 10.1016/j.ctrv.2018.07.004
   PubMed Web of Science ®Google Scholar
• Zhu H, Yu X, Zhang S, Shu K. (2021). Targeting the Complement Pathway in Malignant Glioma Microenvironments. Front Cell Dev Biol, 9 657472 10.3389/fcell.2021.657472
   PubMed Web of Science ®Google Scholar
• Farkas I, Baranyi L, Ishikawa Y, Okada N, Bohata C, Budai D, Fukuda A, Imai M, Okada H. (2002). CD59 blocks not only the insertion of C9 into MAC but inhibits ion channel formation by homologous C5b-8 as well as C5b-9. J Physiol, 539(Pt 2), 537–45. 10.1113/jphysiol.2001.013381
   PubMed Web of Science ®Google Scholar
• Panyutich A V, Szold O, Poon P H, Tseng Y, Ganz T. (1994). Identification of defensin binding to C1 complement. FEBS Lett, 356(2–3), 169–73. 10.1016/0014-5793(94)01261-x
   PubMed Web of Science ®Google Scholar
• Berlov M N, Umnyakova E S, Leonova T S, Milman B L, Krasnodembskaya A D, Ovchinnikova T V, Kokryakov V N. (2015). [Interaction of Arenicin-1 with C1q Protein]. Bioorg Khim, 41(6), 664–8. 10.1134/s1068162015060035
   PubMedGoogle Scholar
• Nauta A J, Daha M R, Tijsma O, van de Water B, Tedesco F, Roos A. (2002). The membrane attack complex of complement induces caspase activation and apoptosis. Eur J Immunol, 32(3), 783–92. 10.1002/1521-4141(200203)32:3<783::AID-IMMU783>3.0.CO;2-Q
   PubMed Web of Science ®Google Scholar
• Posey J Timothy, Soloway M S, Ekici S, Sofer M, Civantos F, Duncan R C, Lokeshwar V B. (2003). Evaluation of the prognostic potential of hyaluronic acid and hyaluronidase (HYAL1) for prostate cancer. Cancer Res, 63(10), 2638–44.
   PubMed Web of Science ®Google Scholar
• Rooney P, Kumar S, Ponting J, Wang M. (1995). The role of hyaluronan in tumour neovascularization (review). Int J Cancer, 60(5), 632–6. 10.1002/ijc.2910600511
   PubMed Web of Science ®Google Scholar
• Cooper B M, Iegre J, O' Donovan D H, Ölwegård Halvarsson M, Spring D R. (2021). Peptides as a platform for targeted therapeutics for cancer: peptide-drug conjugates (PDCs). Chem Soc Rev, 50(3), 1480–1494. 10.1039/d0cs00556h
   PubMed Web of Science ®Google Scholar
• Alas M, Saghaeidehkordi A, Kaur K. (2021). Peptide-Drug Conjugates with Different Linkers for Cancer Therapy. J Med Chem, 64(1), 216–232. 10.1021/acs.jmedchem.0c01530
   PubMed Web of Science ®Google Scholar
• Ruoslahti E. (1996). RGD and other recognition sequences for integrins. Annu Rev Cell Dev Biol, 12 697–715. 10.1146/annurev.cellbio.12.1.697
   PubMed Web of Science ®Google Scholar
• Temming K, Schiffelers R M, Molema G, Kok R J. (2005). RGD-based strategies for selective delivery of therapeutics and imaging agents to the tumour vasculature. Drug Resist Updat, 8(6), 381–402. 10.1016/j.drup.2005.10.002
   PubMed Web of Science ®Google Scholar
• Yang B, Gao J, Pei Q, Xu H, Yu H. (2020). Engineering Prodrug Nanomedicine for Cancer Immunotherapy. Adv Sci (Weinh), 7(23), 2002365 10.1002/advs.202002365
   PubMedGoogle Scholar
• Zhang C, Wu W, Li R, Qiu W, Zhuang Z, Cheng S and Zhang X. (2018). Peptide‐Based Multifunctional Nanomaterials for Tumor Imaging and Therapy. Adv. Funct. Mater., 28(50), 1804492 10.1002/adfm.201804492
   Web of Science ®Google Scholar
• Ngambenjawong C, Chan L W, Fleming H E, Bhatia S N. (2022). Conditional Antimicrobial Peptide Therapeutics. ACS Nano, 16(10), 15779–15791. 10.1021/acsnano.2c04162
   PubMedGoogle Scholar
• Jana A, Narula P, Chugh A, Kulshreshtha R. (2019). Efficient delivery of anti-miR-210 using Tachyplesin, a cell penetrating peptide, for glioblastoma treatment. Int J Pharm, 572 118789 10.1016/j.ijpharm.2019.118789
   PubMedGoogle Scholar
• Grainger D W, van der Mei H C, Jutte P C, van den Dungen J J, Schultz M J, van der Laan B F, Zaat S A, Busscher H J. (2013). Critical factors in the translation of improved antimicrobial strategies for medical implants and devices. Biomaterials, 34(37), 9237–43. 10.1016/j.biomaterials.2013.08.043
   PubMed Web of Science ®Google Scholar
• Xue Q et al . (2018). Anti-infective biomaterials with surface-decorated tachyplesin I. Biomaterials, 178 351–362. 10.1016/j.biomaterials.2018.05.008
   PubMed Web of Science ®Google Scholar
• Shen D, Pouliot L M, Hall M D, Gottesman M M. (2012). Cisplatin resistance: a cellular self-defense mechanism resulting from multiple epigenetic and genetic changes. Pharmacol Rev, 64(3), 706–21. 10.1124/pr.111.005637
   PubMed Web of Science ®Google Scholar
• Trendowski M R, El Charif O, Dinh P C, Travis L B, Dolan M Eileen. (2019). Genetic and Modifiable Risk Factors Contributing to Cisplatin-induced Toxicities. Clin Cancer Res, 25(4), 1147–1155. 10.1158/1078-0432.CCR-18-2244
   PubMed Web of Science ®Google Scholar
• Wang A, Zheng Y, Zhu W, Yang L, Yang Y, Peng J. (2022). Melittin-Based Nano-Delivery Systems for Cancer Therapy. Biomolecules, 12(1),– 10.3390/biom12010118
   Web of Science ®Google Scholar
• Greten F R, Grivennikov S I. (2019). Inflammation and Cancer: Triggers, Mechanisms, and Consequences. Immunity, 51(1), 27–41. 10.1016/j.immuni.2019.06.025
   PubMed Web of Science ®Google Scholar
• Karin M, Lawrence T, Nizet V. (2006). Innate immunity gone awry: linking microbial infections to chronic inflammation and cancer. Cell, 124(4), 823–35. 10.1016/j.cell.2006.02.016
   PubMed Web of Science ®Google Scholar
• Narunsky-Haziza L et al . (2022). Pan-cancer analyses reveal cancer-type-specific fungal ecologies and bacteriome interactions. Cell, 185(20), 3789–3806.e17. 10.1016/j.cell.2022.09.005
   PubMed Web of Science ®Google Scholar
• Dohlman A B, Klug J, Mesko M, Gao I H, Lipkin S M, Shen X, Iliev I D. (2022). A pan-cancer mycobiome analysis reveals fungal involvement in gastrointestinal and lung tumors. Cell, 185(20), 3807–3822.e12. 10.1016/j.cell.2022.09.015
   PubMed Web of Science ®Google Scholar
• Muttenthaler M, King G F, Adams D J, Alewood P F. (2021). Trends in peptide drug discovery. Nat Rev Drug Discov, 20(4), 309–325.
   PubMed Web of Science ®Google Scholar
• Ruoslahti E. (1996). RGD and other recognition sequences for integrins. Annu Rev Cell Dev Biol, 12 697–715. 10.1146/annurev.cellbio.12.1.697
   PubMed Web of Science ®Google Scholar