Inhibitory and antimicrobial activities of OGTI and HV-BBI peptides, fragments and analogs derived from amphibian skin

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• 作者：Dawid D臋bowski^a ; ^{ddebowski@chem.univ.gda.pl} ; Rafa艂 艁ukajtis^a ; Anna 艁臋gowska^a ; Natalia Karna^a ; Micha艂 Piku艂a^b ; Magdalena Wysocka^a ; Irena Maliszewska^c ; Marcin Sie艅czyk^c ; Adam Lesner^a ; Krzysztof Rolka^a
• 关键词：Inhibitor ; Serine proteinases ; Peptomer ; Peptide ; Amphibian skin
• 刊名：Peptides
• 出版年：2012
• 期刊代码：59_01969781
• 类别：neu
• 出版时间：June, 2012
• 卷：35
• 期：2
• 页码：276-284
• 文件大小：696 K

摘要

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 尾-trypsin, bovine 伪-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 [Phe⁸]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.