Antimicrobial, cytotoxic, and insulin-releasing activities of the amphibian host-defense peptide ocellatin-3N and its L-lysine-substituted analogs.
Mice
Animals
Humans
Antimicrobial Cationic Peptides
/ chemistry
Lysine
Anti-Bacterial Agents
/ chemistry
Diabetes Mellitus, Type 2
/ metabolism
Carcinoma, Non-Small-Cell Lung
/ metabolism
Endothelial Cells
/ metabolism
Amphibian Proteins
/ pharmacology
Gram-Positive Bacteria
Gram-Negative Bacteria
Lung Neoplasms
/ metabolism
Anti-Infective Agents
Insulin
/ metabolism
Antineoplastic Agents
/ pharmacology
Anura
/ metabolism
Skin
/ metabolism
Leptodactylidae
antimicrobial peptide
cytotoxicity
diabetes
frog skin
insulin release
Journal
Journal of peptide science : an official publication of the European Peptide Society
ISSN: 1099-1387
Titre abrégé: J Pept Sci
Pays: England
ID NLM: 9506309
Informations de publication
Date de publication:
Apr 2023
Apr 2023
Historique:
revised:
12
11
2022
received:
17
10
2022
accepted:
22
11
2022
pubmed:
26
11
2022
medline:
8
3
2023
entrez:
25
11
2022
Statut:
ppublish
Résumé
The host-defense peptide ocellatin-3N (GIFDVLKNLAKGVITSLAS.NH
Substances chimiques
Antimicrobial Cationic Peptides
0
Lysine
K3Z4F929H6
Anti-Bacterial Agents
0
Amphibian Proteins
0
Anti-Infective Agents
0
Insulin
0
Antineoplastic Agents
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e3463Subventions
Organisme : Ulster University Strategic Funding, Northern Ireland Department of Education and Learning
Informations de copyright
© 2022 The Authors. Journal of Peptide Science published by European Peptide Society and John Wiley & Sons Ltd.
Références
Erspamer V, Vialli M. Presence of enteramine in the skin of Amphibia. Nature. 1951;167(4260):1033. doi:10.1038/1671033a0
Xu X, Lai R. The chemistry and biological activities of peptides from amphibian skin secretions. Chem Rev. 2015;115(4):1760-1846. doi:10.1021/cr4006704
Conlon JM, Mechkarska M, Leprince J. Peptidomic analysis in the discovery of therapeutically valuable peptides in amphibian skin secretions. Expert Rev Proteomics. 2019;16(11-12):897-908. doi:10.1080/14789450.2019.1693894
Gaiser RA, Ayerra Mangado J, Mechkarska M, et al. Selection of antimicrobial frog peptides and temporin-1DRa analogues for treatment of bacterial infections based on their cytotoxicity and differential activity against pathogens. Chem Biol Drug des. 2020;96(4):1103-1113. doi:10.1111/cbdd.13569
Raaymakers C, Verbrugghe E, Hernot S, et al. Antimicrobial peptides in frog poisons constitute a molecular toxin delivery system against predators. Nat Commun. 2017;8(1):1495. doi:10.1038/s41467-017-01710-1
Tran TTN, Tran DP, Nguyen VC, Tran TDT, Bui TTT, Bowie JH. Antioxidant activities of major tryptophyllin L peptides: a joint investigation of Gaussian-based 3D-QSAR and radical scavenging experiments. J Pept Sci. 2021;27(4):e3295. doi:10.1002/psc.3295
Wang S, Feng C, Yin S, et al. A novel peptide from the skin of amphibian Rana limnocharis with potency to promote skin wound repair. Nat Prod Res. 2021;35(20):3514-3518. doi:10.1080/14786419.2019.1710702
Pantic JM, Jovanovic IP, Radosavljevic GD, Arsenijevic NN, Conlon JM, Lukic ML. The potential of frog skin-derived peptides for development into therapeutically-valuable immunomodulatory agents. Molecules. 2017;22(12):E2071. doi:10.3390/molecules22122071
Dong Z, Hu H, Yu X, et al. Novel frog skin-derived peptide Dermaseptin-PP for lung cancer treatment: in vitro/vivo evaluation and anti-tumor mechanisms study. Front Chem. 2020;8:476. doi:10.3389/fchem.2020.00476
Musale V, Guilhaudis L, Abdel-Wahab YHA, Flatt PR, Conlon JM. Insulinotropic activity of the host-defense peptide frenatin 2D: conformational, structure-function and mechanistic studies. Biochimie. 2019;156:12-21. doi:10.1016/j.biochi.2018.09.008
Musale V, Moffett RC, Owolabi B, Conlon JM, Flatt PR, Abdel-Wahab YHA. Mechanisms of action of the antidiabetic peptide [S4K]CPF-AM1 in db/db mice. J Mol Endocrinol. 2021;66(2):115-128. doi:10.1530/JME-20-0152
Frost DR. Amphibian species of the world: an online reference. Version 6.1. American Museum of Natural History. 2021. https://amphibiansoftheworld.amnh.org/index.php. 10.5531/db.vz.0001
Conlon JM. A proposed nomenclature for antimicrobial peptides from frogs of the genus Leptodactylus. Peptides. 2008;29(9):1631-1632. doi:10.1016/j.peptides.2008.04.016. accessed October 1, 2022.
Gomes KAGG, Dos Santos DM, Santos VM, et al. NMR structures in different membrane environments of three ocellatin peptides isolated from Leptodactylus labyrinthicus. Peptides. 103:72-83. doi:10.1016/j.peptides.2018.03.016
Sousa JC, Berto RF, Gois EA, et al. Leptoglycin: a new glycine/leucine-rich antimicrobial peptide isolated from the skin secretion of the South American frog Leptodactylus pentadactylus (Leptodactylidae). Toxicon. 2009;54(1):23-32. doi:10.1016/j.toxicon.2009.03.011
Conlon JM, Abdel-Wahab YH, Flatt PR, et al. A glycine-leucine-rich peptide structurally related to the plasticins from skin secretions of the frog Leptodactylus laticeps (Leptodactylidae). Peptides. 2009;30(5):888-892. doi:10.1016/j.peptides.2009.01.008
Barran G, Kolodziejek J, Coquet L, et al. Peptidomic analysis of skin secretions of the Caribbean frogs Leptodactylus insularum and Leptodactylus nesiotus (Leptodactylidae) identifies an ocellatin with broad spectrum antimicrobial activity. Antibiotics (Basel). 2020;9(10):718. doi:10.3390/antibiotics9100718
Kyte J, Doolittle DF. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982;157(1):105-132. doi:10.1016/0022-2836(82)90515-0
Clinical Laboratory and Standards Institute. Methods for Dilution Antimicrobial Susceptibility Tests for Bacteria That Grow Aerobically. CLSI Standard M07. 11thed. CLSI; 2018.
Clinical Laboratory and Standards Institute. Reference Method for Broth Dilution Antifungal Susceptibility Testing of Yeast. CLSI Standard M27. 4thed. CLS1; 2017.
Grieco P, Carotenuto A, Auriemma L, et al. The effect of D-amino acid substitution on the selectivity of temporin L towards target cells: identification of a potent anti-Candida peptide. Biochim Biophys Acta. 2013;1828(2):652-660. doi:10.1016/j.bbamem.2012.08.027
Conlon JM, Attoub S, Musale V, et al. Isolation and characterization of cytotoxic and insulin-releasing components from the venom of the black-necked spitting cobra Naja nigricollis (Elapidae). Toxicon X. 2020;6:100030. doi:10.1016/j.toxcx.2020.100030
McClenaghan NH, Barnett CR, Ah-Sing E, et al. Characterization of a novel glucose-responsive insulin-secreting cell line, BRIN-BD11, produced by electrofusion. Diabetes. 1996;45(8):1132-1140. doi:10.2337/diab.45.8.1132
Conlon JM, Moffett RC, Leprince J, Flatt PR. Identification of components in frog skin secretions with therapeutic potential as antidiabetic agents. Methods Mol Biol. 2018;1719:319-333. doi:10.1007/978-1-4939-7537-2_21
Flatt PR, Bailey CJ. Abnormal plasma glucose and insulin responses in heterozygous lean (ob/+) mice. Diabetologia. 1981;20(5):573-577. doi:10.1007/BF00252768
Miguel JC, Patterson S, Abdel-Wahab YH, Mathias PC, Flatt PR. Time-correlation between membrane depolarization and intracellular calcium in insulin secreting BRIN-BD11 cells: studies using FLIPR. Cell Calcium. 2004;36(1):43-50. doi:10.1016/j.ceca.2003.11.007
Han Y, Zhang M, Lai R, Zhang Z. Chemical modifications to increase the therapeutic potential of antimicrobial peptides. Peptides. 2021;146:170666. doi:10.1016/j.peptides.2021.170666
Kabelka I, Vácha R. Advances in molecular understanding of α-helical membrane-active peptides. Acc Chem Res. 2021;54(9):2196-2204. doi:10.1021/acs.accounts.1c00047
Gottler LM, Ramamoorthy A. Structure, membrane orientation, mechanism, and function of pexiganan-a highly potent antimicrobial peptide designed from magainin. Biochim Biophys Acta. 2009;1788(8):1680-1686. doi:10.1016/j.bbamem.2008.10.009
Pál T, Sonnevend A, Galadari S, Conlon JM. Design of potent, non-toxic antimicrobial agents based upon the structure of the frog skin peptide, pseudin-2. Regul Pept. 2005;129(1-3):85-91. doi:10.1016/j.regpep.2005.01.015
Conlon JM, Mechkarska M, Arafat K, Attoub S, Sonnevend A. Analogues of the frog skin peptide alyteserin-2a with enhanced antimicrobial activities against Gram-negative bacteria. J Pept Sci. 2012;18(4):270-275. doi:10.1002/psc.2397
Muñoz V, Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. Nat Struct Biol. 1994;1(6):399-409. doi:10.1038/nsb0694-399
Sliman R, Rehm S, Shlaes DM. Serious infections caused by Bacillus species. Medicine (Baltimore). 1987;66(3):218-223. doi:10.1097/00005792-198705000-00005
Reynolds D, Kollef M. The epidemiology and pathogenesis and treatment of Pseudomonas aeruginosa infections: an update. Drugs. 2021;81(18):2117-2131. doi:10.1007/s40265-021-01635-6
Qin J, Yang H, Shan Z, Jiang L, Zhang Q. Clinical efficacy and safety of antifungal drugs for the treatment of Candida parapsilosis infections: a systematic review and network meta-analysis. J Med Microbiol. 2021;70(10):001434. doi:10.1099/jmm.0.001434
Mader JS, Hoskin DW. Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment. Expert Opin Investig Drugs. 2006;15(8):933-946. doi:10.1517/13543784.15.8.933
Conlon JM, Mechkarska M, Lukic ML, Flatt PR. Potential therapeutic applications of multifunctional host-defense peptides from frog skin as anti-cancer, anti-viral, immunomodulatory, and anti-diabetic agents. Peptides. 2014;57:67-77. doi:10.1016/j.peptides.2014.04.019
Choromańska A, Chwiłkowska A, Kulbacka J, et al. Modifications of plasma membrane organization in cancer cells for targeted therapy. Molecules. 2021;26(7):1850. doi:10.3390/molecules26071850
Kondejewski LH, Lee DL, Jelokhani-Niaraki M, Farmer SW, Hancock RE, Hodges RS. Optimization of microbial specificity in cyclic peptides by modulation of hydrophobicity within a defined structural framework. J Biol Chem. 2002;277(1):67-74. doi:10.1074/jbc.M107825200
Kahn SE. The relative contributions of insulin resistance and beta-cell dysfunction to the pathophysiology of Type 2 diabetes. Diabetologia. 2003;46(1):3-19. doi:10.1007/s00125-003-1190-9
Conlon JM, Mechkarska M, Abdel-Wahab YH, Flatt PR. Peptides from frog skin with potential for development into agents for Type 2 diabetes therapy. Peptides. 2018;100:275-281. doi:10.1016/j.peptides.2017.09.001
Idevall-Hagren O, Tengholm A. Metabolic regulation of calcium signalling in beta cells. Semin Cell Dev Biol. 2020;103:20-30. doi:10.1016/j.semcdb.2020.01.008
Sarmiento BE, Santos Menezes LF, Schwartz EF. Insulin release mechanism modulated by toxins isolated from animal venoms: from basic research to drug development prospects. Molecules. 2019;24(10):1846. doi:10.3390/molecules24101846
Owolabi BO, Ojo OO, Srinivasan DK, Conlon JM, Flatt PR, Abdel-Wahab YH. In vitro and in vivo insulinotropic properties of the multifunctional frog skin peptide hymenochirin-1B: a structure-activity study. Amino Acids. 2016;48(2):535-547. doi:10.1007/s00726-015-2107-x
Conlon JM, Flatt PR, Bailey CJ. Recent advances in peptide-based therapy for Type 2 diabetes and obesity. Peptides. 2021;145:170652. doi:10.1016/j.peptides.2021.170652
Carey IM, Critchley JA, DeWilde S, Harris T, Hosking FJ, Cook DG. Risk of infection in Type 1 and Type 2 diabetes compared with the general population: a matched cohort study. Diabetes Care. 2018;41(3):513-521. doi:10.2337/dc17-2131