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Journal 'Cytokines & inflammation', 2012, No. 2

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Original Articles

Number 2'2012

The biological activity of proline-rich host defense peptides of the innate immune system

E.V. Yamschikova, D.S. Orlov, N.I. Kolodkin, M.S. Zharkova, T.Yu. Pazina, G.A. Sakuta, A.S. Trulev, V.N. Kokryakov, O.V. Shamova

Antimicrobial peptides (AMPs) are the key effector molecules of animal and human innate immune system. Proline-rich antimicrobial peptides (PRP) comprise a special group of AMPs whose members have a potent antimicrobial activity and low toxicity towards mammalian cells and therefore can be considered as promising templates for development of new antibiotic drugs. However the features of AMPs of this group remain poorly explored. In the present work, the results of a comparative study of the biological activity of two natural proline-rich peptides (PRP) of the bactenecins family — ChBac3.4 and ChBac5 are presented. Despite a significant structural similarity, the biological activity of these peptides was different. While ChBac5 demonstrated properties, typical of PRP (its antimicrobial action was not accompanied by marked damaging of bacterial membranes and it showed a low toxicity towards human cells), another peptide — ChBac3.4 caused considerably higher increase in the inner membrane permeabilization of E .coli ML35p and, in contrast to ChBac5, was toxic towards some tumor cell lines in culture. Such differences might be due to higher hydrophobicity of ChBac3.4 molecule in comparison with ChBac5 and a lack of polyproline helix conformation, typical of most PRP. It was also shown that both peptides possessed similar lipopolysaccharide-binding activity, and low hemolytic features for human erythrocytes. In addition, ChBac5, but not ChBac3.4, induced proliferation of human fibroblasts. The obtained results provide valuable information for future detailed structure-activity relationship study directed to a design of novel therapeutic agents on the basis of the studied PRP. (Cytokines and Inflammation. 2012. Vol. 11. № 2. P. 100–106.)

Keywords: antimicrobial peptides, bactenecins, Bac3.

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