title: Inhibitory and antimicrobial activities of OGTI and HV-BBI peptides, fragments and analogs derived from amphibian skin.
abstract: A series of linear and cyclic fragments and analogs of two peptides (OGTI and HV-BBI) isolated from skin secretions of frogs were synthesized by the solid-phase method. Their inhibitory activity against several serine proteinases: bovine β-trypsin, bovine α-chymotypsin, human leukocyte elastase and cathepsin G from human neutrophils, was investigated together with evaluation of their antimicrobial activities against Gram-negative bacteria (Escherichia coli) and Gram-positive species isolated from patients (Staphylococcus aureus, Staphylococcus epidermidis, Enterococcus sp., Streptococcus sp.). The cytotoxicity of the selected peptides toward an immortal human skin fibroblast cell line was also determined. Three peptides: HV-BBI, its truncated fragment HV-BBI(3-18) and its analog [Phe(8)]HV-BBI can be considered as bifunctional compounds with inhibitory as well as antibacterial properties. OGTI, although it did not display trypsin inhibitory activity as previously reported in the literature, exerted antimicrobial activity toward S. epidermidis. In addition, under our experimental conditions, this peptide did not show cytotoxicity.
authors.affiliation: Department of Bioorganic Chemistry, University of Gdansk, Gdansk, Poland. ddebowski@chem.univ.gda.pl
authors.forename: Dawid
authors.initials: D
authors.lastname: Dębowski
authors.forename: Rafał
authors.initials: R
authors.lastname: Łukajtis
authors.forename: Anna
authors.initials: A
authors.lastname: Łęgowska
authors.forename: Natalia
authors.initials: N
authors.lastname: Karna
authors.forename: Michał
authors.initials: M
authors.lastname: Pikuła
authors.forename: Magdalena
authors.initials: M
authors.lastname: Wysocka
authors.forename: Irena
authors.initials: I
authors.lastname: Maliszewska
authors.forename: Marcin
authors.initials: M
authors.lastname: Sieńczyk
authors.forename: Adam
authors.initials: A
authors.lastname: Lesner
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Rolka
mesh_terms: D029845:Amphibian Proteins / Q000737:chemistry / Q000494:pharmacology* / Q000633:toxicity; D000818:Animals; D000890:Anti-Infective Agents / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000494:pharmacology* / Q000633:toxicity; D001001:Anura; D056649:Cathepsin G / Q000037:antagonists & inhibitors / Q000187:drug effects; D002460:Cell Line; D049109:Cell Proliferation / Q000187:drug effects; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D016983:Enterococcus / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects; D006801:Humans; D019272:Leukocyte Elastase / Q000037:antagonists & inhibitors; D008826:Microbial Sensitivity Tests; D009504:Neutrophils / Q000187:drug effects; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology* / Q000633:toxicity; D012867:Skin / Q000378:metabolism; D013210:Staphylococcus / Q000187:drug effects; D013291:Streptococcus / Q000187:drug effects; D014357:Trypsin / Q000187:drug effects; D014361:Trypsin Inhibitors
chemical_list: D029845:Amphibian Proteins; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; C529612:HV-BBI peptide, Huia versabilis; D010455:Peptides; D014361:Trypsin Inhibitors; D002918:Chymotrypsin; C117608:alpha-chymotrypsin; D056649:Cathepsin G; D019272:Leukocyte Elastase; D014357:Trypsin