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 beta-trypsin, bovine alpha-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. (c) 2012 Elsevier Inc. All rights reserved.
Authors
- Dawid Dębowski,
- dr Rafał Łukajtis link open in new tab ,
- Anna Łęgowska,
- Natalia Karna,
- Michał Pikuła,
- Magdalena Wysocka,
- Irena Maliszewska,
- Marcin Sieńczyk,
- Adam Lesner link open in new tab ,
- Krzysztof Rolka
Additional information
- DOI
- Digital Object Identifier link open in new tab 10.1016/j.peptides.2012.04.001
- Category
- Publikacja w czasopiśmie
- Type
- artykuł w czasopiśmie wyróżnionym w JCR
- Language
- angielski
- Publication year
- 2012
