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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

The Influence of Isoleucine and Arginine on Biological Activity and Peptide- Membrane Interactions of Antimicrobial Peptides from the Bactericidal Domain of AvBD4

Author(s): Wan-Ning Hu, Wen-Jing Jiao, Zhi Ma, Na Dong, Qing-Quan Ma, Chang-Xuan Shao and An-Shan Shan

Volume 20, Issue 11, 2013

Page: [1189 - 1199] Pages: 11

DOI: 10.2174/09298665113209990042

Price: $65


In this study, the influence of isoleucine and arginine on the biological activity and peptide-membrane interactions of linear avian β-defensin-4 (RL38) analogs was investigated. Results of biological activities showed that the antimicrobial activities of AvBD-4 analogs were closely related to hydrophobicity and amphipathicity. The peptide GLI19 with high hydrophobicity value and amphipathicity displayed broad spectrum antimicrobial activity against both gram-negative and gram-positive, whereas GLR19 with increasing multiple charges only exhibited activity against gram-negative. The interaction between peptides and the liposome membrane demonstrated that the peptides preferentially bound to negatively charged phospholipids over zwitterionic phospholipids, which supported the antimicrobial activity data. The outer membranes assay further demonstrated that GLI19 had a greater capacity than the other tested peptides to penetrate the cell membrane at a low concentration. Collectively, the peptides derived from the bactericidal domain of linear β- defensins by truncation and hydrophobic amino acid substitution may be effective high-potential antibacterial agents.

Keywords: Antimicrobial peptides, biological activity, peptide-membrane interactions, cell selectivity, avian β-defensin-4.

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