References
- Mada, S. B.; Ugwu, C. P.; Abarshi, M. M. Health Promoting Effects of Food-Derived Bioactive Peptides: A Review. Int. J. Pept. Res. Ther. 2019, 26(2), 831–848. DOI: 10.1007/s10989-019-09890-8.
- Brown, T. D.; Whitehead, K. A.; Mitragotri, S. Materials for Oral Delivery of Proteins and Peptides. Nat. Rev. Mater. 2019, 5(2), 127–148. DOI: 10.1038/s41578-019-0156-6.
- Dubey, S. K., Parab, S., Dabholkar, N., Agrawal, M., Singhvi, G., Alexander, A., Bapat, R. A., Kesharwani, P.; et al. Oral Peptide Delivery: Challenges and the Way Ahead. Drug Discov. Today. 2021, 26(4), 931–950.
- Sánchez, A.; Vázquez, A. Bioactive Peptides: A Review. Food Qual. Saf. 2017, 1(1), 29–46. DOI: 10.1093/fqs/fyx006.
- Kim, S.-K.; Wijesekara, I. Development and Biological Activities of Marine-Derived Bioactive Peptides: A Review. J. Funct. Foods. 2010, 2(1), 1–9. DOI: 10.1016/j.jff.2010.01.003.
- Cicero, A. F. G.; Fogacci, F.; Colletti, A. Potential Role of Bioactive Peptides in Prevention and Treatment of Chronic Diseases: A Narrative Review. Br. J. Pharmacol. 2017, 174(11), 1378–1394. DOI: 10.1111/bph.13608.
- Zizzari, A. T., Pliatsika, D., Gall, F. M., Fischer, T., Riedl, R.; et al. New Perspectives in Oral Peptide Delivery. Drug Discov. Today. 2021, 26(4), 1097–1105.
- Segura-Campos, M., Chel-Guerrero, L., Betancur-Ancona, D., Hernandez-Escalante, V. M.; et al. Bioavailability of Bioactive Peptides. Food Rev. Int. 2011, 27(3), 213–226.
- Siklos, M.; BenAissa, M.; Thatcher, G. R. Cysteine Proteases as Therapeutic Targets: Does Selectivity Matter? a Systematic Review of Calpain and Cathepsin Inhibitors. Acta Pharm. Sin. B. 2015, 5(6), 506–519. DOI: 10.1016/j.apsb.2015.08.001.
- Park, K.; Kwon, I. C.; Park, K. Oral Protein Delivery: Current Status and Future Prospect. React. Funct. Polym. 2011, 71(3), 280–287. DOI: 10.1016/j.reactfunctpolym.2010.10.002.
- Ganesh, A. N.; Heusser, C.; Garad, S.; Sánchez-Félix, M. V., et al. Patient-Centric Design for Peptide Delivery: Trends in Routes of Administration and Advancement in Drug Delivery Technologies. Med. Drug Discovery. 2021, 9, 100079. DOI: 10.1016/j.medidd.2020.100079.
- Zhu, Q., Chen, Z., Paul, P. K., Lu, Y., Wu, W., Qi, J.; et al. Oral Delivery of Proteins and Peptides: Challenges, Status Quo and Future Perspectives. Acta Pharm. Sin. B. 2021, 11(8), 2416–2448.
- Chakrabarti, S.; Guha, S.; Majumder, K. Food-Derived Bioactive Peptides in Human Health: Challenges and Opportunities. Nutrients. 2018, 10(11), 1738. DOI: 10.3390/nu10111738.
- Leksrisompong, P., Gerard, P., Lopetcharat, K., Drake, M.; et al. Bitter Taste Inhibiting Agents for Whey Protein Hydrolysate and Whey Protein Hydrolysate Beverages. J. Food Sci. 2012, 77(8), S282–287.
- Ishibashi, N.; Kubo, T.; Chino, M.; Fukui, H.; Shinoda, I. Studies on Flavored Peptides. Part IV. Taste of Proline-Containing Peptides. Agric. Biol. Chem. 1988, 52(1), 95–98. DOI: 10.1271/bbb1961.52.95.
- Iwaniak, A., Hrynkiewicz, M., Bucholska, J., Minkiewicz, P., Darewicz, M.; et al. Understanding the Nature of Bitter-Taste di- and Tripeptides Derived from Food Proteins Based on Chemometric Analysis. J. Food Biochem. 2019, 43(1), e12500.
- Zhao, C. J.; Schieber, A.; Ganzle, M. G. Formation of Taste-Active Amino Acids, Amino Acid Derivatives and Peptides in Food Fermentations - a Review. Food. Res. Int. 2016, 89(Pt 1), 39–47. DOI: 10.1016/j.foodres.2016.08.042.
- Norio, I.; Yasuhiro, A.; Hidenori, K.; Katsushige, K., and Hideo. Bitterness of Leucine-Containing Peptides. Agric. Biol. Chem. 1987, 51(9), 2389–2394. DOI: 10.1271/bbb1961.51.2389.
- Ishibashi, N., et al. Bitterness of Phenylalanine- and Tyrosine-Containing Peptides. Agric Biol Chem 2016, 51(12), 3309–3313. DOI: 10.1080/00021369.1987.10868574.
- Appalaraju Jaggupilli, R. H.; Upadhyaya, J. D.; Bhullar, R. P.; Chelikani, P. Bitter Taste Receptors: Novel Insights into the Biochemistry and pharmacology. Int. J. Biochem. Cell Biol. 2016, 77, 184–196. DOI: 10.1016/j.biocel.2016.03.005.
- Chunlei Zhang, M. A.; Singh, N.; Liu, K.; Chelikani, P.; Aluko, R. E. Beef Protein-Derived Peptides as Bitter Taste Receptor T2R4 Blockers. J. Agric. Food Chem. 2018, 66(19), 4902–4912. DOI: 10.1021/acs.jafc.8b00830.
- Min Jung Kim, H. J. S.; Kim, Y.; Misaka, T. Mee-Ra Rhyu Umami–bitter Interactions: The Suppression of Bitterness by Umami Peptides via Human Bitter Taste Receptor. Biochem. Biophys. Res. Commun. 2015, 456(2), 586–590. DOI: 10.1016/j.bbrc.2014.11.114.
- Qingbiao Xu, N. S.; Hong, H.; Yan, X.; Yu, W.; Jiang, X.; Chelikani, P.; Wu, J. Hen Protein-Derived Peptides as the Blockers of Human Bitter Taste Receptors T2R4, T2R7 and T2R14. Food Chem. 2019, 283, 621–627. DOI: 10.1016/j.foodchem.2019.01.059.
- Whitcomb, D. C.; Lowe, M. E. Human Pancreatic Digestive Enzymes. Dig. Dis. Sci. 2007, 52(1), 1–17. DOI: 10.1007/s10620-006-9589-z.
- Brayden, D. J., Hill, T. A., Fairlie, D. P., Maher, S., Mrsny, R. J.; et al. Systemic Delivery of Peptides by the Oral Route: Formulation and Medicinal Chemistry Approaches. Adv. Drug Deliv. Rev. 2020, 157, 2–36. DOI: 10.1016/j.addr.2020.05.007.
- Karasov, W. H.; Douglas, A. E. Comparative Digestive Physiology. Compr. Physiol. 2013, 3(2), 741–783. DOI: 10.1002/cphy.c110054.
- Vagiannis, D., Yu, Z., Novotna, E., Morell, A., Hofman, J.; et al. Entrectinib Reverses Cytostatic Resistance Through the Inhibition of ABCB1 Efflux Transporter, but Not the CYP3A4 Drug-Metabolizing Enzyme. Biochem Pharmacol. 2020, 178, 114061. DOI: 10.1016/j.bcp.2020.114061.
- Homayun, B.; Lin, X.; Choi, H. J. Challenges and Recent Progress in Oral Drug Delivery Systems for Biopharmaceuticals. Pharmaceutics. 2019, 11(3), 129. DOI: 10.3390/pharmaceutics11030129.
- Hellinger, R.; Gruber, C. W. Peptide-Based Protease Inhibitors from Plants. Drug Discov. Today. 2019, 24(9), 1877–1889. DOI: 10.1016/j.drudis.2019.05.026.
- Wagner, C. E.; Wheeler, K. M.; Ribbeck, K. Mucins and Their Role in Shaping the Functions of Mucus Barriers. Annu. Rev. Cell Dev. Biol. 2018, 34, 189–215. DOI: 10.1146/annurev-cellbio-100617-062818.
- Liu, L., Tian, C., Dong, B., Xia, M., Cai, Y., Hu, R., Chu, X.; et al. Models to Evaluate the Barrier Properties of Mucus During Drug Diffusion. Int. J. Pharm. 2021, 599, 120415. DOI: 10.1016/j.ijpharm.2021.120415.
- Arike, L.; Seiman, A.; van der Post, S.; Rodriguez Piñeiro, A. M.; Ermund, A.; Schütte, A.; Bäckhed, F.; Johansson, M. E. V.; Hansson, G. C., et al. Protein Turnover in Epithelial Cells and Mucus Along the Gastrointestinal Tract is Coordinated by the Spatial Location and Microbiota. Cell Rep. 2020, 30(4), 1077–1087 e1073.
- Yildiz, H. M., Speciner, L., Ozdemir, C., Cohen, D. E., Carrier, R. L.; et al. Food-Associated Stimuli Enhance Barrier Properties of Gastrointestinal Mucus. Biomaterials. 2015, 54, 1–8. DOI: 10.1016/j.biomaterials.2015.02.118.
- de Santa Barbara, P.; van den Brink, G. R.; Roberts, D. J. Development and Differentiation of the Intestinal Epithelium. Cell. Mol. Life Sci. 2003, 60(7), 1322–1332. DOI: 10.1007/s00018-003-2289-3.
- Ensign, L. M.; Cone, R.; Hanes, J. Oral Drug Delivery with Polymeric Nanoparticles: The Gastrointestinal Mucus Barriers. Adv. Drug Deliv. Rev. 2012, 64(6), 557–570. DOI: 10.1016/j.addr.2011.12.009.
- Boyd, B. J.; Bergström, C. A. S.; Vinarov, Z.; Kuentz, M.; Brouwers, J.; Augustijns, P.; Brandl, M.; Bernkop-Schnürch, A.; Shrestha, N.; Préat, V., et al. Successful Oral Delivery of Poorly Water-Soluble Drugs Both Depends on the Intraluminal Behavior of Drugs and of Appropriate Advanced Drug Delivery Systems. Eur. J. Pharm. Sci. 2019, 137, 104967. DOI: 10.1016/j.ejps.2019.104967.
- Drucker, D. J. Advances in Oral Peptide Therapeutics. Nat. Rev. Drug Discov. 2020, 19(4), 277–289. DOI: 10.1038/s41573-019-0053-0.
- Craik, D. J., Fairlie, D. P., Liras, S., Price, D.; et al. The Future of Peptide-Based Drugs. Chem. Biol. Drug Des. 2013, 81(1), 136–147.
- Ismail, R.; Csoka, I. Novel Strategies in the Oral Delivery of Antidiabetic Peptide Drugs - Insulin, GLP 1 and Its Analogs. Eur. J. Pharm. Biopharm. 2017, 115, 257–267. DOI: 10.1016/j.ejpb.2017.03.015.
- VigBs, S. T. R.; Timoszyk, J.K., et al. Human PEPT1 Pharmacophore Distinguishes Between Dipeptide Transport and Binding. J. Med. Chem. 2006, 49(12), 36–44.
- Bougle, D.; Bouhallab, S. Dietary Bioactive Peptides: Human Studies. Crit. Rev. Food Sci. Nutr. 2017, 57(2), 335–343. DOI: 10.1080/10408398.2013.873766.
- Gao Jinjin, G. Y. Intestinal Absorption of Milk-Derived ACE Inhibitory Peptides LL and LPEW Using Caco-2 Cell Model. Food Sci. 2017, 38(11), 214–219. DOI: 10.7506/spkx1002-6630-201711034.
- Wang, B.; Li, B. Effect of Molecular Weight on the Transepithelial Transport and Peptidase Degradation of Casein-Derived Peptides by Using Caco-2 Cell Model. Food Chem. 2017, 218, 1–8. DOI: 10.1016/j.foodchem.2016.08.106.
- Wang, B., Wang, C., Huo, Y., Li, B.; et al. The Absorbates of Positively Charged Peptides from Casein Show High Inhibition Ability of LDL Oxidation in vitro : Identification of Intact Absorbed Peptides. J. Funct. Foods. 2016, 20, 380–393. DOI: 10.1016/j.jff.2015.11.012.
- Hong, S. M., Tanaka, M., Koyanagi, R., Shen, W., Matsui, T.; et al. Structural Design of Oligopeptides for Intestinal Transport Model. J. Agric. Food Chem. 2016, 64(10), 2072–2079.
- Ding, L., Wang, L., Yu, Z., Ma, S., Du, Z., Zhang, T., Liu, J.; et al. Importance of Terminal Amino Acid Residues to the Transport of Oligopeptides Across the Caco-2 Cell Monolayer. J. Agric. Food Chem. 2017, 65(35), 7705–7712.
- Bo Wang, B. L. Charge and Hydrophobicity of Casein Peptides Influence Transepithelial Transport and Bioavailability. Food Chem. 2018, 032(245), 646–652. DOI: 10.1016/j.foodchem.2017.09.032.
- Blanca Hernández-Ledesma, M. D. M. C.; Recio, I. Antihypertensive Peptides: Production, Bioavailability and Incorporation into Foods. Adv. Colloid Interface Sci. 2011, 165, 23–25. DOI: 10.1016/j.cis.2010.11.001.
- Rutherfurd-Markwick, K. J. Food Proteins as a Source of Bioactive Peptides with Diverse Functions. Br. J. Nutr. 2012, 108, S149–S157. DOI: 10.1017/S000711451200253X.
- Miner-Williams, W. M.; Stevens, B. R.; Moughan, P. J. Are Intact Peptides Absorbed from the Healthy Gut in the Adult Human? Nutr. Res. Rev. 2014, 27, 308–329. DOI: 10.1017/S0954422414000225.
- Holzer, P. Opioid Receptors in the Gastrointestinal Tract. Regul. Pept. 2009, 155, 11–17. DOI: 10.1016/j.regpep.2009.03.012.
- Bao, X.; Wu, J. Impact of Food-Derived Bioactive Peptides on Gut Function and Health. Food. Res. Int. 2021, 147, 110485. DOI: 10.1016/j.foodres.2021.110485.
- Nana Isobe, M. S.; Oda, M.; Tanabe, S. Enzyme-Modified Cheese Exerts Inhibitory Effects on Allergen Permeation in Rats Suffering from Indomethacin-Induced Intestinal Inflammation. Biosci. Biotechnol., Biochem. 2008, 72(7), 1740–1745. DOI: 10.1271/bbb.80042.
- Gian Carlo Tenore, E. P.; Lama, S.; Vanacore, D.; Di Maro, S.; Maisto, M.; Capasso, R.; Merlino, F.; Borrelli, F.; Stiuso, P.; Novellino, E. Intestinal Anti-Inflammatory Effect of a Peptide Derived from Gastrointestinal Digestion of Buffalo (Bubalus Bubalis) Mozzarella Cheese. Nutrients. 2019, 11(3), 610. DOI: 10.3390/nu11030610.
- Juliette Caron, D. D.; Dhulster, P.; Ravallec, R.; Cudennec, B. Protein Digestion-Derived Peptides and the Peripheral Regulation of Food Intake. Front. Endocrinol. 2017, 8(85). DOI: 10.3389/fendo.2017.00085.
- Xu, Q., Hong, H., Wu, J., Yan, X.; et al. Bioavailability of Bioactive Peptides Derived from Food Proteins Across the Intestinal Epithelial Membrane: A Review. Trends Food Sci. Technol. 2019, 86, 399–411. DOI: 10.1016/j.tifs.2019.02.050.
- Brandsch, M. Transport of Drugs by Proton-Coupled Peptide Transporters: Pearls and Pitfalls. Expert Opin. Drug Metab. Toxicol. 2009, 5(8), 887–905. DOI: 10.1517/17425250903042292.
- Pedretti, A.; De Luca, L.; Marconi, C.; Negrisoli, G.; Aldini, G.; Vistoli, G., et al. Modeling of the Intestinal Peptide Transporter hPept1 and Analysis of Its Transport Capacities by Docking and Pharmacophore Mapping. ChemMedchem. 2008, 3(12), 1913–1921.
- Bolger, M. B.; Haworth, I. S.; Yeung, A. K.; Ann, D., von Grafenstein, H., Hamm-Alvarez, S., Okamoto, C. T., Kim, K.-J., Basu, S. K., Wu, S. Structure, function, and Molecular Modeling Approaches to the Study of the Intestinal Dipeptide Transporter PepT1. J. Pharm. Sci. 1998, 87(16), 1286–1291. DOI: 10.1021/js980090u.
- Brandsch, M.; Knutter, I.; Bosse-Doenecke, E. Pharmaceutical and Pharmacological Importance of Peptide Transporters. J. Pharm. Pharmacol. 2008, 60(5), 543–585. DOI: 10.1211/jpp.60.5.0002.
- Brodin, B. U. N. C.; Steffansen, B.; Frokjaer, S. Transport of Peptidomimetic Drugs by the Intestinal di/tri-Peptide Transporter, PepT1. Acta Pharmacol. Toxicol. 2002, 90, 285–296.
- Miyako Okamura, T. T.; Katsura, T.; Saito, H.; Inui, K.-I. Inhibitory Effect of Zinc on PEPT1-Mediated Transport of Glycylsarcosine and Beta-Lactam Antibiotics in Human Intestinal Cell Line Caco-2. Pharm. Res. 2003, 20, 1389–1393. DOI: 10.1023/A:1025797808703.
- Newstead, S. Recent Advances in Understanding Proton Coupled Peptide Transport via the POT Family. Curr. Opin. Struct. Biol. 2017, 45, 17–24. DOI: 10.1016/j.sbi.2016.10.018.
- Satake, M., Enjoh, M., Nakamura, Y., Takano, T., Kawamura, Y., Arai, S., Shimizu, M.; et al. Transepithelial Transport of the Bioactive Tripeptide, Val-Pro-Pro, in Human Intestinal Caco-2 Cell Monolayers. Biosci., Biotechnol., Biochem. 2014, 66(2), 378–384.
- Gleeson, J. P.; Frías, J. M.; Ryan, S. M.; Brayden, D. J., et al. Sodium Caprate Enables the Blood Pressure-Lowering Effect of Ile-Pro-Pro and Leu-Lys-Pro in Spontaneously Hypertensive Rats by Indirectly Overcoming PepT1 Inhibition. Eur. J. Pharm. Biopharm. 2018, 128, 179–187. DOI: 10.1016/j.ejpb.2018.04.021.
- Lei, L.; Sun, H.; Liu, D.; Liu, L.; Li, S. Transport of Val-Leu-Pro-Val-Pro in Human Intestinal Epithelial (Caco-2) Cell Monolayers. J. Agric. Food Chem. 2008, 56, 3582–3586. DOI: 10.1021/jf703640p.
- Zhang, T., Su, M., Jiang, X., Xue, Y., Zhang, J., Zeng, X., Wu, Z., Guo, Y., Pan, D.; et al. Transepithelial Transport Route and Liposome Encapsulation of Milk-Derived ACE-Inhibitory Peptide Arg-Leu-Ser-Phe-Asn-Pro. J. Agric. Food Chem. 2019, 67(19), 5544–5551.
- Del Mar Contreras, M., Sancho, A. I., Recio, I., Mills, C.; et al. Absorption of Casein Antihypertensive Peptides Through an in vitro Model of Intestinal Epithelium. Food Digest. 2012, 3(1–3), 16–24.
- Bejjani, S.; Wu, J. Transport of IRW, an Ovotransferrin-Derived Antihypertensive Peptide, in Human Intestinal Epithelial Caco-2 Cells. J. Agric. Food Chem. 2013, 61(7), 1487–1492. DOI: 10.1021/jf302904t.
- Xu, Q., Fan, H., Yu, W., Hong, H., Wu, J.; et al. Transport Study of Egg-Derived Antihypertensive Peptides (LKP and IQW) Using Caco-2 and HT29 Coculture Monolayers. J. Agric. Food Chem. 2017, 65(34), 7406–7414.
- Zuisu, C. R. D. G. Y. Absorption Mechanism of Cod Skin Collagen Peptide in Caco-2 Cell Monolayer Model. Food Sci. 2018, 39(19), 154–161. DOI: 10.7506/spkx1002-6630-201819024.
- Salamat-Miller, N.; Johnston, T. P. Current Strategies Used to Enhance the Paracellular Transport of Therapeutic Polypeptides Across the Intestinal Epithelium. Int. J. Pharm. 2005, 294(1–2), 201–216. DOI: 10.1016/j.ijpharm.2005.01.022.
- Brunner, J.; Ragupathy, S.; Borchard, G. Target Specific Tight Junction Modulators. Adv. Drug Deliv. Rev. 2021, 171, 266–288. DOI: 10.1016/j.addr.2021.02.008.
- Xue Haiyan, X. L.; BaoyuaN, H. ACE Inhibitory Activity and Intestinal Absorption of Milk Casein Hydrolysates by in vitro Simulated Digestion. Modern Food Sci. Technol. 2018, 34(6), 9–17. DOI: 10.13982/j.mfst.1673-9078.2018.6.002.
- Ding, L., Wang, L., Yu, Z., Zhang, T., Liu, J.; et al. Digestion and Absorption of an Egg White ACE-Inhibitory Peptide in Human Intestinal Caco-2 Cell Monolayers. Int. J. Food Sci. Nutr. 2016, 67(2), 111–116.
- Salama, N. N.; Eddington, N. D.; Fasano, A. Tight Junction Modulation and Its Relationship to Drug Delivery. Adv. Drug Deliv. Rev. 2006, 58(1), 15–28. DOI: 10.1016/j.addr.2006.01.003.
- Tanabe, S. Short Peptide Modules for Enhancing Intestinal Barrier Function. Curr. Pharm. Des. 2012, 18, 776–781. DOI: 10.2174/138161212799277653.
- Li, Y., Zhao, J., Liu, X., Xia, X., Wang, Y., Zhou, J.; et al. Transport of a Novel Angiotensin-I-Converting Enzyme Inhibitory Peptide Ala-His-Leu-Leu Across Human Intestinal Epithelial Caco-2 Cells. J. Med. Food. 2017, 20(3), 243–250.
- Shimizu, M.; Soichi Arai, M. T. Transepithelial Transport of Oligopeptides in the Human Intestinal Cell, Caco-2. Peptides. 1997, 18, 681–687. DOI: 10.1016/S0196-9781(97)00002-8.
- Vij, R., Reddi, S., Kapila, S., Kapila, R.; et al. Transepithelial Transport of Milk Derived Bioactive Peptide VLPVPQK. Food Chem. 2016, 190, 681–688. DOI: 10.1016/j.foodchem.2015.05.121.
- Sienkiewicz-Szłapka, E.; Jarmołowska, B.; Krawczuk, S.; Kostyra, E.; Kostyra, H.; Bielikowicz, K., et al. Transport of Bovine Milk-Derived Opioid Peptides Across a Caco-2 Monolayer. Int. Dairy J. 2009, 19(4), 252–257.
- Xu, F., Wang, L., Ju, X., Zhang, J., Yin, S., Shi, J., He, R., Yuan, Q.; et al. Transepithelial Transport of YWDHNNPQIR and Its Metabolic Fate with Cytoprotection Against Oxidative Stress in Human Intestinal Caco-2 Cells. J. Agric. Food Chem. 2017, 65(10), 2056–2065.
- Makvandi, P., Chen, M., Sartorius, R., Zarrabi, A., Ashrafizadeh, M., Dabbagh Moghaddam, F., Ma, J., Mattoli, V., Tay, F. R.; et al. Endocytosis of Abiotic Nanomaterials and Nanobiovectors: Inhibition of Membrane Trafficking. Nano Today. 2021, 40, 101279. DOI: 10.1016/j.nantod.2021.101279.
- Fan, W., Xia, D., Zhu, Q., Hu, L., Gan, Y.; et al. Intracellular Transport of Nanocarriers Across the Intestinal Epithelium. Drug Discov. Today. 2016, 21(5), 856–863.
- Komin, A., et al. Peptide-Based Strategies for Enhanced Cell Uptake, Transcellular Transport, and Circulation: Mechanisms and Challenges. Adv. Drug Deliv. Rev. 2017, 110-111, 52–64. DOI: 10.1016/j.addr.2016.06.002.
- Beloqui, A.; des Rieux, A.; Preat, V. Mechanisms of Transport of Polymeric and Lipidic Nanoparticles Across the Intestinal Barrier. Adv. Drug Deliv. Rev. 2016, 106(Pt B), 242–255. DOI: 10.1016/j.addr.2016.04.014.
- Khan, M. M.; Filipczak, N.; Torchilin, V. P. Cell Penetrating Peptides: A Versatile Vector for Co-Delivery of Drug and Genes in Cancer. J. Control Release. 2021, 330, 1220–1228. DOI: 10.1016/j.jconrel.2020.11.028.
- Regazzo, D.; Mollé, D.; Gabai, G.; Tomé, D.; Dupont, D.; Leonil, J.; Boutrou, R., et al. The (193-209) 17-Residues Peptide of Bovine β-Casein is Transported Through Caco-2 Monolayer. Mol. Nutr. Food Res. 2010, 54(10), 1428–1435.
- Sai, Y.; Kajita, M.; Tamai, I., Wakama, J., Wakamiya, T., Tsuji, A. et al. Adsorptive-Mediated Endocytosis of a Basic Peptide in Enterocyte-Like Caco-2 Cells. Am. J. Physiol. 1998, 275. DOI:10.1152/ajpgi.1998.275.3.G514.
- Ding, L., Wang, L., Zhang, T., Yu, Z., Liu, J.; et al. Hydrolysis and Transepithelial Transport of Two Corn Gluten Derived Bioactive Peptides in Human Caco-2 Cell Monolayers. Food. Res. Int. 2018, 106, 475–480. DOI: 10.1016/j.foodres.2017.12.080.
- Miguel, M.; Dávalos, A.; Manso, M. A.; de la Peña, G.; Lasunción, M. A.; López-Fandiño, R., et al. Transepithelial Transport Across Caco-2 Cell Monolayers of Antihypertensive Egg-Derived Peptides. PepT1-Mediated Flux of Tyr-Pro-Ile. Mol. Nutr. Food Res. 2008, 52(12), 1507–1513.
- Xing, L., Liu, R., Tang, C., Pereira, J., Zhou, G., Zhang, W.; et al. The Antioxidant Activity and Transcellular Pathway of Asp-Leu-Glu-Glu in a Caco-2 Cell Monolayer. Int. J. Food Sci. Technol. 2018, 53(10), 2405–2414.
- Gleeson, J. P.; Brayden, D. J.; Ryan, S. M. Evaluation of PepT1 Transport of Food-Derived Antihypertensive Peptides, Ile-Pro-Pro and Leu-Lys-Pro Using in Vitro, ex vivo and in vivo Transport Models. Eur. J. Pharm. Biopharm. 2017, 115, 276–284. DOI: 10.1016/j.ejpb.2017.03.007.
- Guo, Y., Gan, J., Zhu, Q., Zeng, X., Sun, Y., Wu, Z., Pan, D.; et al. Transepithelial Transport of Milk-Derived Angiotensin I-Converting Enzyme Inhibitory Peptide with the RLSFNP Sequence. J. Sci. Food Agric. 2018, 98(3), 976–983.
- Ma, L., and Lu, K. J., Synthesis of ACE Inhibitory Peptide KVLPVP and Its Mimic Peptides. Advances in Biomedical Engineering–Proceedings of 2011 International Conference on Agricultural and Biosystems Engineering, Amsterdam, Netherlands, 2011.
- Yu, Z., Wu, S., Zhao, W., Ding, L., Fan, Y., Shiuan, D., Liu, J., Chen, F.; et al. Anti-Alzheimer's Activity and Molecular Mechanism of Albumin-Derived Peptides Against AChE and BChE. Food Funct. 2018, 9(2), 1173–1178.
- Ding, L., Zhang, Y., Jiang, Y., Wang, L., Liu, B., Liu, J.; et al. Transport of Egg White ACE-Inhibitory Peptide, Gln-Ile-Gly-Leu-Phe, in Human Intestinal Caco-2 Cell Monolayers with Cytoprotective Effect. J. Agric. Food Chem. 2014, 62(14), 3177–3182.
- Eckert, E.; Zambrowicz, A.; Pokora, M.; Setner, B.; Dąbrowska, A.; Szołtysik, M.; Szewczuk, Z.; Polanowski, A.; Trziszka, T.; Chrzanowska, J., et al. Egg-Yolk Protein By-Product as a Source of ACE-Inhibitory Peptides Obtained with Using Unconventional Proteinase from Asian Pumpkin (Cucurbita Ficifolia). J. Proteomics. 2014, 110, 107–116. DOI: 10.1016/j.jprot.2014.08.003.
- Zhang, J., et al. Isolation and Identification of Antioxidative Peptides from Rice Endosperm Protein Enzymatic Hydrolysate by Consecutive Chromatography and MALDI-TOF/TOF MS/MS. Food Chem. 2010, 119(1), 226–234.
- Quirós, A., et al. Bioavailability of the Antihypertensive Peptide LHLPLP: Transepithelial Flux of HLPLP. Int. Dairy J. 2008, 18(3), 279–286. DOI: 10.1016/j.idairyj.2007.09.006.
- Batista, P., et al. Recent Insights in the Use of Nanocarriers for the Oral Delivery of Bioactive Proteins and Peptides. Peptides 2018, 101, 112–123. DOI: 10.1016/j.peptides.2018.01.002.
- Maher, S.; Mrsny, R. J.; Brayden, D. J. Intestinal Permeation Enhancers for Oral Peptide Delivery. Adv. Drug Deliv. Rev. 2016, 106(Pt B), 277–319. DOI: 10.1016/j.addr.2016.06.005.
- Maher, S., et al. Application of Permeation Enhancers in Oral Delivery of Macromolecules: An Update. Pharmaceutics. 2019, 11(1). DOI:10.3390/pharmaceutics11010041.
- Thanou, M.; Verhoef, J. C.; Junginger, H. E. Chitosan and Its Derivatives as Intestinal Absorption Enhancers. Adv. Drug Delivery Rev. 2001, 50, 91–101.
- Dahlgren, D., et al. Effect of Paracellular Permeation Enhancers on Intestinal Permeability of Two Peptide Drugs, Enalaprilat and Hexarelin, in Rats. Acta Pharm. Sin. B 2021, 11(6), 1667–1675. DOI: 10.1016/j.apsb.2020.12.019.
- Rehmani, S.; Dixon, J. E. Oral Delivery of Anti-Diabetes Therapeutics Using Cell Penetrating and Transcytosing Peptide Strategies. Peptides. 2018, 100, 24–35. DOI: 10.1016/j.peptides.2017.12.014.
- Nakase, I.; Tanaka, G.; Futaki, S. Cell-Penetrating Peptides (CPPs) as a Vector for the Delivery of siRnas into Cells. Mol. BioSyst. 2013, 9(5), 855–861. DOI: 10.1039/c2mb25467k.
- Mariko, M.; Isao, et al. Site-Dependent Effect of Aprotinin, Sodium Caprate, Na2edta and Sodium Glycocholate on Intestinal Absorption of Insulin. Biol. Pharm. Bull. 1993, 16(1), 68–72.
- Cruz-Huerta, E., et al. The Protective Role of the Bowman-Birk Protease Inhibitor in Soybean Lunasin Digestion: The Effect of Released Peptides on Colon Cancer Growth. Food Funct. 2015, 6(8), 2626–2635. DOI: 10.1039/c5fo00454c.
- Renukuntla, J., et al. Approaches for Enhancing Oral Bioavailability of Peptides and Proteins. Int. J. Pharm. 2013, 447(1–2), 75–93. DOI: 10.1016/j.ijpharm.2013.02.030.
- Leitner, V. M. E. A. Thiolated Polymers: Evidence for the Formation of Disulphide Bonds with Mucus Glycoproteins. Eur. J. Pharm. Biopharm. 2003, 56, 207–214. DOI: 10.1016/S0939-6411(03)00061-4.
- Mansuri, S., et al. Mucoadhesion: A Promising Approach in Drug Delivery System. React. Funct. Polym. 2016, 100, 151–172. DOI: 10.1016/j.reactfunctpolym.2016.01.011.
- Martau, G. A.; Mihai, M.; Vodnar, D. C. The Use of Chitosan, Alginate, and Pectin in the Biomedical and Food Sector-Biocompatibility, Bioadhesiveness, and Biodegradability. Polymers (Basel). 2019, 11(11). DOI: 10.3390/polym11111837.
- Tm, M. W.; Lau, W. M.; Khutoryanskiy, V. V. Chitosan and Its Derivatives for Application in Mucoadhesive Drug Delivery Systems. Polymers (Basel). 2018, 10(3). DOI: 10.3390/polym10030267.
- Ibrahim, Y. H. Y., et al. Review of Recently Used Techniques and Materials to Improve the Efficiency of Orally Administered Proteins/peptides. Daru 2020, 28(1), 403–416. DOI: 10.1007/s40199-019-00316-w.
- Andreani, T., et al. Effect of Mucoadhesive Polymers on the in vitro Performance of Insulin-Loaded Silica Nanoparticles: Interactions with Mucin and Biomembrane Models. Eur. J. Pharm. Biopharm. 2015, 93, 118–126. DOI: 10.1016/j.ejpb.2015.03.027.
- Jørgensen, J. R., et al. Microcontainers for Oral Insulin Delivery – in vitro Studies of Permeation Enhancement. Eur. J. Pharm. Biopharm. 2019, 143, 98–105. DOI: 10.1016/j.ejpb.2019.08.011.
- Su, F. Y., et al. Protease Inhibition and Absorption Enhancement by Functional Nanoparticles for Effective Oral Insulin Delivery. Biomaterials 2012, 33(9), 2801–2811. DOI: 10.1016/j.biomaterials.2011.12.038.
- Leone-Bay, A.; Brayden, D.; Creed, E.; O’Connell, A.; Leipold, H.; Agarwal, R. Heparin Absorption Across the Intestine: Effects of Sodium N[8-(2-Hydroxybenzoyl) Amino] Caprylate in Rat in situ Intestinal Instillations and in Caco-2 Monolayers. Pharm. Res. 1997, 14(12), 1772–1779.
- McGavigan, A. K.; Murphy, K. G. Gut Hormones: The Future of Obesity Treatment? Br.J. Clin. Pharmacol. 2012, 74(6), 911–919. DOI: 10.1111/j.1365-2125.2012.04278.x.
- Gopalakrishnan, S., et al. Mechanism of Action of ZOT-Derived Peptide AT-1002, a Tight Junction Regulator and Absorption Enhancer. Int. J. Pharm. 2009, 365(1–2), 121–130. DOI: 10.1016/j.ijpharm.2008.08.047.
- Zhang, L., et al. The Use of Low Molecular Weight Protamine to Enhance Oral Absorption of Exenatide. Int. J. Pharm. 2018, 547(1–2), 265–273. DOI: 10.1016/j.ijpharm.2018.05.055.
- Haddadzadegan, S.; Dorkoosh, F.; Bernkop-Schnurch, A. Oral Delivery of Therapeutic Peptides and Proteins: Technology Landscape of Lipid-Based Nanocarriers. Adv. Drug Deliv. Rev. 2022, 182, 114097. DOI: 10.1016/j.addr.2021.114097.
- Dhirendra Kumar Malik, S. B.; Ahuja, A.; Hasan, S.; Ali, J. Recent Advances in Protein and Peptide Drug Delivery Systems. Curr. Drug Delivery. 2007, 4(2), 141–151.
- Sonia, T. A.; Rekha, M. R.; Sharma, C. P. Bioadhesive Hydrophobic Chitosan Microparticles for Oral Delivery of Insulin: In vitro Characterization and in vivo Uptake Studies. J. Appl. Polym. Sci. 2011, 119(5), 2902–2910. DOI: 10.1002/app.32979.
- Harloff-Helleberg, S., et al. Exploring the Mucoadhesive Behavior of Sucrose Acetate Isobutyrate: A Novel Excipient for Oral Delivery of Biopharmaceuticals. Drug. Deliv. 2019, 26(1), 532–541. DOI: 10.1080/10717544.2019.1606866.
- Greimel, A.; Werle, M.; Bernkop-Schnurch, A. Oral Peptide Delivery: In-Vitro Evaluation of Thiolated Alginate/poly(acrylic Acid) Microparticles. J. Pharm. Pharmacol. 2007, 59(9), 1191–1198. DOI: 10.1211/jpp.59.9.0002.
- Buckley, S. T.; Hubalek, F.; Rahbek, U. L. Chemically Modified Peptides and Proteins - Critical Considerations for Oral Delivery. Tissue Barriers. 2016, 4(2), e1156805. DOI: 10.1080/21688370.2016.1156805.
- Makhlof, A., Fujimoto, S., Tozuka, Y., Takeuchi, H.; et al. In vitro and in vivo Evaluation of Wga–carbopol Modified Liposomes as Carriers for Oral Peptide Delivery. Eur. J. Pharm. Biopharm. 2011, 77(2), 216–224.
- Zhao, S., Li, J., Wang, F., Yu, T., Zhou, Y., He, L., Zhang, Y., Yang, J.; et al. Semi-Elastic Core-Shell Nanoparticles Enhanced the Oral Bioavailability of Peptide Drugs. Chin. Chem. Lett. 2020, 31(5), 1147–1152.
- Menzel, C.; Holzeisen, T.; Laffleur, F.; Zaichik, S.; Abdulkarim, M.; Gumbleton, M.; Bernkop-Schnürch, A., et al. In vivo Evaluation of an Oral Self-Emulsifying Drug Delivery System (SEDDS) for Exenatide. J. Control Release. 2018, 277, 165–172. DOI: 10.1016/j.jconrel.2018.03.018.
- Sharma, G., Wilson, K., van der Walle, C. F., Sattar, N., Petrie, J. R., Ravi Kumar, M. N. V.; et al. Microemulsions for Oral Delivery of Insulin: Design, Development and Evaluation in Streptozotocin Induced Diabetic Rats. Eur. J. Pharm. Biopharm. 2010, 76(2), 159–169.
- Sheng, J., Han, L., Qin, J., Ru, G., Li, R., Wu, L., Cui, D., Yang, P., He, Y., Wang, J.; et al. N -Trimethyl Chitosan Chloride-Coated PLGA Nanoparticles Overcoming Multiple Barriers to Oral Insulin Absorption. ACS Appl. Mater. Interfaces. 2015, 7(28), 15430–15441.
- Han, Y., Gao, Z., Chen, L., Kang, L., Huang, W., Jin, M., Wang, Q., Bae, Y. H.; et al. Multifunctional Oral Delivery Systems for Enhanced Bioavailability of Therapeutic Peptides/proteins. Acta Pharm. Sin. B. 2019, 9(5), 902–922.
- Mero, A., Schiavon, M., Veronese, F. M., Pasut, G.; et al. A New Method to Increase Selectivity of Transglutaminase Mediated Pegylation of Salmon Calcitonin and Human Growth Hormone. J. Control Release. 2011, 154(1), 27–34.
- Wu, L., Chen, J., Wu, Y., Zhang, B., Cai, X., Zhang, Z., Wang, Y., Si, L., Xu, H., Zheng, Y.; et al. Precise and Combinatorial Pegylation Generates a Low-Immunogenic and Stable Form of Human Growth Hormone. J. Control Release. 2017, 249, 84–93. DOI: 10.1016/j.jconrel.2017.01.029.
- Lawrence, P. B.; Price, J. L. How Pegylation Influences Protein Conformational Stability. Curr. Opin. Chem. Biol. 2016, 34, 88–94. DOI: 10.1016/j.cbpa.2016.08.006.
- Han-Mei, W.-B.-Z.-Y.-C.-Y.-Y.-X. Studies on the Pegylation Conditions of Polypeptide CPU-HM and Pharmacodynamics of Modified Products in vivo. Pharm. Biotechnol. 2016, 23(4), 313–317.
- Arnesen, T. Towards a Functional Understanding of Protein N-Terminal Acetylation. PLoS Biol. 2011, 9(5), e1001074. DOI: 10.1371/journal.pbio.1001074.
- Colgrave, M. L. C. D. J., Craik, D. J. Thermal, Chemical, and Enzymatic Stability of the Cyclotide Kalata B1: The Importance of the Cyclic Cystine Knot. Biochemistry. 2004, 43, 5965–5975. DOI: 10.1021/bi049711q.
- Nielsen, D. S., Shepherd, N. E., Xu, W., Lucke, A. J., Stoermer, M. J., Fairlie, D. P.; et al. Orally Absorbed Cyclic Peptides. Chem. Rev. 2017, 117(12), 8094–8128.
- Miklavzin, A.; Cegnar, M.; Kerč, J.; Kristl, J., et al. Effect of Surface Hydrophobicity of Therapeutic Protein Loaded in Polyelectrolyte Nanoparticles on Transepithelial Permeability. Acta. Pharm. 2018, 68(3), 275–293.
- Choonara, B. F., Choonara, Y. E., Kumar, P., Bijukumar, D., du Toit, L. C., Pillay, V.; et al. A Review of Advanced Oral Drug Delivery Technologies Facilitating the Protection and Absorption of Protein and Peptide Molecules. Biotechnol. Adv. 2014, 32(7), 1269–1282.
- Jiang, X., Pan, D., Tao, M., Zhang, T., Zeng, X., Wu, Z., Guo, Y.; et al. New Nanocarrier System for Liposomes Coated with Lactobacillus Acidophilus S-Layer Protein to Improve Leu–gln–pro–glu Absorption Through the Intestinal Epithelium. J. Agric. Food Chem. 2021, 69(27), 7593–7602.
- Mohan, A.; McClements, D. J.; Udenigwe, C. C. Encapsulation of Bioactive Whey Peptides in Soy Lecithin-Derived Nanoliposomes: Influence of Peptide Molecular Weight. Food Chem. 2016, 213, 143–148. DOI: 10.1016/j.foodchem.2016.06.075.
- Mohan, A., Rajendran, S. R. C. K., Thibodeau, J., Bazinet, L., Udenigwe, C. C.; et al. Liposome Encapsulation of Anionic and Cationic Whey Peptides: Influence of Peptide Net Charge on Properties of the Nanovesicles. Lwt. 2018, 87, 40–46. DOI: 10.1016/j.lwt.2017.08.072.
- da Rosa Zavareze, E.; Telles, A. C.; Mello El Halal, S. L.; da Rocha, M.; Colussi, R.; Marques de Assis, L.; Suita de Castro, L. A.; Guerra Dias, A. R.; Prentice-Hernández, C., et al. Production and Characterization of Encapsulated Antioxidative Protein Hydrolysates from Whitemouth Croaker (Micropogonias Furnieri) Muscle and Byproduct. LWT - Food Sci. Technol. 2014, 59(2), 841–848.
- Mosquera, M.; Giménez, B.; da Silva, I. M.; Boelter, J. F.; Montero, P.; Gómez-Guillén, M. C.; Brandelli, A., et al. Nanoencapsulation of an Active Peptidic Fraction from Sea Bream Scales Collagen. Food Chem. 2014, 156, 144–150. DOI: 10.1016/j.foodchem.2014.02.011.
- Mosquera, M.; Giménez, B.; Montero, P.; Gómez-Guillén, M. C., et al. Incorporation of Liposomes Containing Squid Tunic ACE-Inhibitory Peptides into Fish Gelatin. J. Sci. Food Agric. 2016, 96(3), 769–776.
- da Silva Malheiros, P.; Micheletto, Y. M. S.; Silveira, N. P. D.; Brandelli, A., et al. Development and Characterization of Phosphatidylcholine Nanovesicles Containing the Antimicrobial Peptide Nisin. Food Res. Int. 2010, 43(4), 1198–1203.
- Yokota, D.; Moraes, M.; Pinho, S. C. Characterization of Lyophilized Liposomes Produced with Non-Purified Soy Lecithin: A Case Study of Casein Hydrolysate Microencapsulation. Braz. J. Chem. Eng. 2012, 29(2), 325–335. DOI: 10.1590/S0104-66322012000200013.
- Maherani, B., Arab-Tehrany, E., Kheirolomoom, A., Cleymand, F., Linder, M.; et al. Influence of Lipid Composition on Physicochemical Properties of Nanoliposomes Encapsulating Natural Dipeptide Antioxidant L-Carnosine. Food Chem. 2012, 134(2), 632–640.
- Pugliese, R., Bollati, C., Gelain, F., Arnoldi, A., Lammi, C.; et al. A Supramolecular Approach to Develop New Soybean and Lupin Peptide Nanogels with Enhanced Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Activity. J. Agric. Food Chem. 2019, 67(13), 3615–3623.
- Gong, K. J., Shi, A.-M., Liu, H.-Z., Liu, L., Hu, H., Yang, Y., Adhikari, B., Wang, Q.; et al. Preparation of Nanoliposome Loaded with Peanut Peptide Fraction: Stability and Bioavailability. Food Funct. 2016, 7(4), 2034–2042.
- Mazloomi, S. N., et al. Physicochemical Properties of Chitosan-Coated Nanoliposome Loaded with Orange Seed Protein Hydrolysate. J. Food Eng. 2020, 280. DOI: 10.1016/j.jfoodeng.2020.109976.
- Li, Z.; Paulson, A. T.; Gill, T. A. Encapsulation of Bioactive Salmon Protein Hydrolysates with Chitosan-Coated Liposomes. J. Funct. Foods. 2015, 19, 733–743. DOI: 10.1016/j.jff.2015.09.058.
- Ramezanzade, L.; Hosseini, S. F.; Nikkhah, M. Biopolymer-Coated Nanoliposomes as Carriers of Rainbow Trout Skin-Derived Antioxidant Peptides. Food Chem. 2017, 234, 220–229. DOI: 10.1016/j.foodchem.2017.04.177.
- Li, N., et al. Multivesicular Liposomes for the Sustained Release of Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Peanuts: Design, Characterization, and in vitro Evaluation. Molecules. 2019, 24(9). DOI:10.3390/molecules24091746.
- Choi, M.-J., Choi, D., Lee, J., Jo, Y.-J., et al. Encapsulation of a Bioactive Peptide in a Formulation of W1/O/W2-Type Double Emulsions: Formation and Stability. Food Struct. 2020, 25. DOI: 10.1016/j.foostr.2020.100145.
- Du, Z., Liu, J., Zhang, T., Yu, Y., Zhang, Y., Zhai, J., Huang, H., Wei, S., Ding, L., Liu, B.; et al. A Study on the Preparation of Chitosan-Tripolyphosphate Nanoparticles and Its Entrapment Mechanism for Egg White Derived Peptides. Food Chem. 2019, 286, 530–536. DOI: 10.1016/j.foodchem.2019.02.012.
- Ilhan-Ayisigi, E., Budak, G., Celiktas, M. S., Sevimli-Gur, C., Yesil-Celiktas, O.; et al. Anticancer Activities of Bioactive Peptides Derived from Rice Husk Both in Free and Encapsulated Form in Chitosan. J. Ind. Eng. Chem. 2021, 103, 381–391. DOI: 10.1016/j.jiec.2021.08.006.
- Su, L., et al. Solid Lipid Nanoparticles Enhance the Resistance of Oat-Derived Peptides That Inhibit Dipeptidyl Peptidase IV in Simulated Gastrointestinal Fluids. J. Funct. Foods. 2020, 65. DOI: 10.1016/j.jff.2019.103773.
- Tan, M. L.; Choong, P. F.; Dass, C. R. Recent Developments in Liposomes, Microparticles and Nanoparticles for Protein and Peptide Drug Delivery. Peptides. 2010, 31(1), 184–193. DOI: 10.1016/j.peptides.2009.10.002.
- Bulbake, U., Doppalapudi, S., Kommineni, N., Khan, W., et al. Liposomal Formulations in Clinical Use: An Updated Review. Pharmaceutics 2017, 9(4). doi:10.3390/pharmaceutics9020012
- Alavi, M.; Karimi, N.; Safaei, M. Application of Various Types of Liposomes in Drug Delivery Systems. Adv. Pharm. Bull. 2017, 7(1), 3–9. DOI: 10.15171/apb.2017.002.
- Xu, Y.; Michalowski, C. B.; Beloqui, A. Advances in Lipid Carriers for Drug Delivery to the Gastrointestinal Tract. Curr. Opin. Colloid Interface Sci. 2021, 52, 101414. DOI: 10.1016/j.cocis.2020.101414.
- Liu, W., Hou, Y., Jin, Y., Wang, Y., Xu, X., Han, J.; et al. Research Progress on Liposomes: Application in Food, Digestion Behavior and Absorption Mechanism. Trends Food Sci. Technol. 2020, 104, 177–189. DOI: 10.1016/j.tifs.2020.08.012.
- Ramezanzade, L., et al. Cross-Linked Chitosan-Coated Liposomes for Encapsulation of Fish-Derived Peptide. Lwt. 2021, 150. DOI: 10.1016/j.lwt.2021.112057.
- Mahmood, A.; Bernkop-Schnurch, A. SEDDS: A Game Changing Approach for the Oral Administration of Hydrophilic Macromolecular Drugs. Adv. Drug Deliv. Rev. 2019, 142, 91–101. DOI: 10.1016/j.addr.2018.07.001.
- Abdulkarim, M.; Sharma, P. K.; Gumbleton, M. Self-Emulsifying Drug Delivery System: Mucus Permeation and Innovative Quantification Technologies. Adv. Drug Deliv. Rev. 2019, 142, 62–74. DOI: 10.1016/j.addr.2019.04.001.
- Czogalla, A. Oral Cyclosporine A–the Current Picture of Its Liposomal and Other Delivery Systems. Cell. Mol. Biol. Lett. 2009, 14(1), 139–152. DOI: 10.2478/s11658-008-0041-6.
- Agrawal, M., Saraf, S., Saraf, S., Dubey, S. K., Puri, A., Patel, R. J., Ravichandiran, V., Murty, U. S., Alexander, A.; et al. Recent Strategies and Advances in the Fabrication of Nano Lipid Carriers and Their Application Towards Brain Targeting. J. Control Release. 2020, 321, 372–415. DOI: 10.1016/j.jconrel.2020.02.020.
- Singh, Y., Meher, J. G., Raval, K., Khan, F. A., Chaurasia, M., Jain, N. K., Chourasia, M. K.; et al. Nanoemulsion: Concepts, Development and Applications in Drug Delivery. J. Control Release. 2017, 252, 28–49. DOI: 10.1016/j.jconrel.2017.03.008.
- Callender, S. P., Mathews, J. A., Kobernyk, K., Wettig, S. D.; et al. Microemulsion Utility in Pharmaceuticals: Implications for Multi-Drug Delivery. Int. J. Pharm. 2017, 526(1–2), 425–442.
- Hu, X. B., Tang, T.-T., Li, Y.-J., Wu, J.-Y., Wang, J.-M., Liu, X.-Y., Xiang, D.-X.; et al. Phospholipid Complex Based Nanoemulsion System for Oral Insulin Delivery: Preparation, in Vitro, and in vivo Evaluations. Int J. Nanomedi. 2019, 14, 3055–3067. DOI: 10.2147/IJN.S198108.
- Gleeson, J. P.; Ryan, S. M.; Brayden, D. J. Oral Delivery Strategies for Nutraceuticals: Delivery Vehicles and Absorption Enhancers. Trends Food Sci. Technol. 2016, 53, 90–101. DOI: 10.1016/j.tifs.2016.05.007.
- McClements, D. J. Nanoemulsion-Based Oral Delivery Systems for Lipophilic Bioactive Components: Nutraceuticals and Pharmaceuticals. Ther. Delivery. 2013a, (4), 841–857. DOI: 10.4155/tde.13.46.
- Moss, D. M., Curley, P., Kinvig, H., Hoskins, C., Owen, A.; et al. The Biological Challenges and Pharmacological Opportunities of Orally Administered Nanomedicine Delivery. Expert Rev. Gastroenterol. Hepatol. 2018, 12(3), 223–236.
- Rostami, E. Progresses in Targeted Drug Delivery Systems Using Chitosan Nanoparticles in Cancer Therapy: A Mini-Review. J. Drug Delivery Sci. Technol. 2020, 58. DOI: 10.1016/j.jddst.2020.101813.
- Alexander, A. E. A., Ajazuddin, M., Swarna, M., Sharma, M., Tripathi, D. K. Polymers and Permeation Enhancers: Specialized Components of Mucoadhesives. Stamford J. Pharm. 2011, 4, 91–95. DOI: 10.3329/sjps.v4i1.8878.
- Roos, C.; Dahlgren, D.; Berg, S.; Westergren, J.; Abrahamsson, B.; Tannergren, C.; Sjögren, E.; Lennernäs, H., et al. In vivo Mechanisms of Intestinal Drug Absorption from Aprepitant Nanoformulations. Mol. Pharm. 2017, 14(12), 4233–4242.
- Khan, J., Alexander, A., ., Saraf, S., Saraf, S.; et al. Exploring the Role of Polymeric Conjugates Toward Anti-Cancer Drug Delivery: Current Trends and Future Projections. Int. J. Pharm. 2018, 548(1), 500–514.
- Song, Y., Shi, Y., Zhang, L., Hu, H., Zhang, C., Yin, M., Chu, L., Yan, X., Zhao, M., Zhang, X.; et al. Synthesis of CSK-DEX-PLGA Nanoparticles for the Oral Delivery of Exenatide to Improve Its Mucus Penetration and Intestinal Absorption. Mol. Pharm. 2019, 16(2), 518–532.
- Toragall, V.; Baskaran, V. Chitosan-Sodium Alginate-Fatty Acid Nanocarrier System: Lutein Bioavailability, Absorption Pharmacokinetics in Diabetic Rat and Protection of Retinal Cells Against H2O2 Induced Oxidative Stress in vitro. Carbohydr. Polym. 2021, 254, 117409. DOI: 10.1016/j.carbpol.2020.117409.
- Li, H., Zhang, Z., Bao, X., Xu, G., Yao, P.; et al. Fatty Acid and Quaternary Ammonium Modified Chitosan Nanoparticles for Insulin Delivery. Colloids Surf. B Biointerfaces. 2018, 170, 136–143. DOI: 10.1016/j.colsurfb.2018.05.063.
- Liu, J., Li, Y., Zhang, H., Liu, S., Yang, M., Cui, M., Zhang, T., Yu, Y., Xiao, H., Du, Z.; et al. Fabrication, Characterization and Functional Attributes of Zein-Egg White Derived Peptides (EWDP)-Chitosan Ternary Nanoparticles for Encapsulation of Curcumin: Role of EWDP. Food Chem. 2021, 372, 131266. DOI: 10.1016/j.foodchem.2021.131266.
- Hosseini, S. F.; Soleimani, M. R.; Nikkhah, M. Chitosan/sodium Tripolyphosphate Nanoparticles as Efficient Vehicles for Antioxidant Peptidic Fraction from Common Kilka. Int. J. Biol. Macromol. 2018, 111, 730–737. DOI: 10.1016/j.ijbiomac.2018.01.023.
- Cuomo, F., et al. In-Vitro Digestion of Curcumin Loaded Chitosan-Coated Liposomes. Colloids Surf. B Biointerfaces. 2018, 168, 29–34. DOI: 10.1016/j.colsurfb.2017.11.047.
- Zhenhua Hu, S. N.; Goel, S.; Hinkle, L. E.; Wu, X.; Li, C.; Ferrari1, M.; Shen, H. Molecular Targeting of FATP4 Transporter for Oral Delivery of Therapeutic Peptide. Science Advances. 2020. DOI: 10.1126/sciadv.aba0145.
- Mendanha, D. V., et al. Microencapsulation of Casein Hydrolysate by Complex Coacervation with Spi/pectin. Food Res. Int. 2009, 42(8), 1099–1104. DOI: 10.1016/j.foodres.2009.05.007.
- Ma, J.-J., et al. Effect of Spray Drying and Freeze Drying on the Immunomodulatory Activity, Bitter Taste and Hygroscopicity of Hydrolysate Derived from Whey Protein Concentrate. LWT - Food Sci. Technol. 2014, 56(2), 296–302. DOI: 10.1016/j.lwt.2013.12.019.
- Wang, Z., et al. The Effect of Rapeseed Protein Structural Modification on Microstructural Properties of Peptide Microcapsules. Food Bioprocess. Technol. 2015, 8(6), 1305–1318. DOI: 10.1007/s11947-015-1472-5.
- Sun, H., et al. Nanostructures Based on Protein Self-Assembly: From Hierarchical Construction to Bioinspired Materials. Nano Today. 2017, 14, 16–41. DOI: 10.1016/j.nantod.2017.04.006.
- Martínez-López, A. L., et al. Protein-Based Nanoparticles for Drug Delivery Purposes. Int. J. Pharmaceutics. 2020, 581. DOI: 10.1016/j.ijpharm.2020.119289.
- Sadeghi, S., et al. Oral Administration of Protein Nanoparticles: An Emerging Route to Disease Treatment. Pharmacol. Res. 2020, 158, 104685. DOI: 10.1016/j.phrs.2020.104685.
- Kou, L., et al. The Endocytosis and Intracellular Fate of Nanomedicines: Implication for Rational Design. Asian J. Pharm. Sci. 2013, 8(1), 1–10. DOI: 10.1016/j.ajps.2013.07.001.
- Ahmad, A.; Khan, J. M.; Haque, S. Strategies in the Design of Endosomolytic Agents for Facilitating Endosomal Escape in Nanoparticles. Biochimie. 2019, 160, 61–75. DOI: 10.1016/j.biochi.2019.02.012.
- Rathore, B., et al. Nanomaterial Designing Strategies Related to Cell Lysosome and Their Biomedical Applications: A Review. Biomaterials 2019, 211, 25–47. DOI: 10.1016/j.biomaterials.2019.05.002.
- Fan, W., et al. Functional Nanoparticles Exploit the Bile Acid Pathway to Overcome Multiple Barriers of the Intestinal Epithelium for Oral Insulin Delivery. Biomaterials 2018, 151, 13–23. DOI: 10.1016/j.biomaterials.2017.10.022.
- Yuan, X., et al. Virus-Like Nonvirus Cationic Liposome for Efficient Gene Delivery via Endoplasmic Reticulum Pathway. ACS Cent. Sci. 2020, 6(2), 174–188. DOI: 10.1021/acscentsci.9b01052.
- Luo, Q., Jiang, M., Kou, L., Zhang, L., Li, G., Yao, Q., Shang, L., Chen, Y.; et al. Ascorbate-Conjugated Nanoparticles for Promoted Oral Delivery of Therapeutic Drugs via Sodium-Dependent Vitamin C Transporter 1 (SVCT1). Artif. Cells Nanomed. Biotechnol. 2018, 46(sup1), 198–208.
- Hubatsch, I.; Ragnarsson, E. G.; Artursson, P. Determination of Drug Permeability and Prediction of Drug Absorption in Caco-2 Monolayers. Nat. Protoc. 2007, 2(9), 2111–2119. DOI: 10.1038/nprot.2007.303.
- Azenha, M. A., et al. Estimation of the Human Intestinal Permeability of Butyltin Species Using the Caco-2 Cell Line Model. Food Chem. Toxicol. 2004, 42(9), 1431–1442. DOI: 10.1016/j.fct.2004.04.004.
- Shen, W.; Matsui, T. Current Knowledge of Intestinal Absorption of Bioactive Peptides. Food Funct. 2017, 8(12), 4306–4314. DOI: 10.1039/c7fo01185g.
- Deferme, S. A.; Augustijns, P. P in Vitro screening Models to Assess Intestinal Drug Absorption and Metabolism. Drug Absorption Stud. 2008, 182–215.
- Wilson, G. H.; Dix, I. F.; Williamson, C. J.; Shah, I.; Mackay, R.; Artursson, M. P Transport and Permeability Properties of Human Caco-2 Cells: An In Vitro Model of the Intestinal Epithelial Cell Barrier. J. Control Release. 1990, 11(1–3), 25–40. DOI: 10.1016/0168-3659(90)90118-D.
- Hilgers, A. R.; Conradi, R. A.; Burton, P. S. Caco-2 Cell Monolayers as a Model for Drug Transport Across the Intestinal Mucosa. Pharm. Res. 1990, 7, 902–910. DOI: 10.1023/A:1015937605100.
- Backhed, F.; Ley, R. E.; Sonnenburg, J. L.; Peterson, D. A.; Gordon, J. I. Host-Bacterial Mutualism in the Human Intestine. Science. 2005, 307, 1915–1920. DOI: 10.1126/science.1104816.
- Zhang, Q., Tong, X., Qi, B., Wang, Z., Li, Y., Sui, X., Jiang, L.; et al. Changes in Antioxidant Activity of Alcalase-Hydrolyzed Soybean Hydrolysate Under Simulated Gastrointestinal Digestion and Transepithelial Transport. J. Funct. Foods. 2018, 42, 298–305. DOI: 10.1016/j.jff.2018.01.017.
- Anderson, R. C., Dalziel, J. E., Haggarty, N. W., Dunstan, K. E., Gopal, P. K., Roy, N. C.; et al. Short Communication: Processed Bovine Colostrum Milk Protein Concentrate Increases Epithelial Barrier Integrity of Caco-2 Cell Layers. J. Dairy Sci. 2019, 102(12), 10772–10778.
- Picariello, G., Iacomino, G., Mamone, G., Ferranti, P., Fierro, O., Gianfrani, C., Di Luccia, A., Addeo, F.; et al. Transport Across Caco-2 Monolayers of Peptides Arising from in vitro Digestion of Bovine Milk Proteins. Food Chem. 2013, 139(1–4), 203–212.
- Lin, K., Ma, Z., Ramachandran, M., De Souza, C., Han, X., Zhang, L.-W.; et al. ACE Inhibitory Peptide KYIPIQ Derived from Yak Milk Casein Induces Nitric Oxide Production in Huvecs and Diffuses via a Transcellular Mechanism in Caco-2 Monolayers. Process Biochem. 2020, 99, 103–111. DOI: 10.1016/j.procbio.2020.08.031.
- Ma, J., Guan, R., Shen, H., Lu, F., Xiao, C., Liu, M., Kang, T.; et al. Comparison of Anticancer Activity Between Lactoferrin Nanoliposome and Lactoferrin in Caco-2 Cells in vitro. Food Chem. Toxicol. 2013, 59, 72–77. DOI: 10.1016/j.fct.2013.05.038.
- Lundquist, P.; Artursson, P. Oral Absorption of Peptides and Nanoparticles Across the Human Intestine: Opportunities, Limitations and Studies in Human Tissues. Adv. Drug Deliv. Rev. 2016, 106(Pt B), 256–276. DOI: 10.1016/j.addr.2016.07.007.
- Rizza, L., Frasca, G., Nicholls, M., Puglia, C., Cardile, V.; et al. Caco-2 Cell Line as a Model to Evaluate Mucoprotective Properties. Int. J. Pharm. 2012, 422(1–2), 318–322.
- Ding, X., Hu, X., Chen, Y., Xie, J., Ying, M., Wang, Y., Yu, Q.; et al. Differentiated Caco-2 Cell Models in Food-Intestine Interaction Study: Current Applications and Future Trends. Trends Food Sci. Technol. 2021, 107, 455–465. DOI: 10.1016/j.tifs.2020.11.015.
- Iftikhar, M., et al. Transport, Metabolism and Remedial Potential of Functional Food Extracts (FFEs) in Caco-2 Cells Monolayer: A Review. Food. Res. Int. 2020, 136, 109240. DOI: 10.1016/j.foodres.2020.109240.
- Rodrigues, D. B.; Failla, M. L. Intestinal Cell Models for Investigating the Uptake, Metabolism and Absorption of Dietary Nutrients and Bioactive Compounds. Curr. Opin. Food Sci. 2021, 41, 169–179. DOI: 10.1016/j.cofs.2021.04.002.
- Vaidyanathan, G., et al. Brush Border Enzyme-Cleavable Linkers: Evaluation for Reducing Renal Uptake of Radiolabeled Prostate-Specific Membrane Antigen Inhibitors. Nucl. Med. Biol. 2018, 62-63, 18–30. DOI: 10.1016/j.nucmedbio.2018.05.002.
- Ahmad, M. K., et al. Oral Administration of a Nephrotoxic Dose of Potassium Bromate, a Food Additive, Alters Renal Redox and Metabolic Status and Inhibits Brush Border Membrane Enzymes in Rats. Food Chem. 2012, 134(2), 980–985. DOI: 10.1016/j.foodchem.2012.03.004.
- Wikman-Larhed, A. A., and Artursson, P. Co-Cultures of Human Intestinal Goblet (HT29-H) and Absorptive (Caco-2) Cells for Studies of Drug and Peptide Absorption. Eur. J. Pharm. 1995, 3(3), 171–183. DOI:10.1016/0928-0987(95)00007-Z .
- Zweibaum, A.; Laburthe, M.; Grasset, E., and Louvard, D. Use of Cultured Cell Lines in Studies of Intestinal Cell Differentiation and Function. Handbook of Physiology. The Gastrointestinal System. Intestinal Absorption and Secretion. 2011, 223–255.