PMID: 22587782May 17, 2012Paper

Novel design of short antimicrobial peptides derived from the bactericidal domain of avian β-defensin-4

Protein and Peptide Letters
Na DongYuzhi Li

Abstract

Short antimicrobial peptides were designed and synthesized by C-terminal truncation and residue substitution of avian β-defensin-4. The biological activity of these peptides was examined to elucidate the quantitative structure-activity relationships and find a lead peptide for the development of a novel antimicrobial peptide. The results showed that the truncation of the avian β-defensin-4 eliminated the hemolysis of the peptide. The GLI13 derivative, developed by substituting the Cys of the truncated peptide with Ile, led to increased antimicrobial activity. These results suggest that the peptides with antimicrobial activity can be derived by truncating the avian β-defensin-4. We further developed the GLI13 derivative with an increased net charge by residue substitution. The results showed that the GLI13-5 with 5 net charges had the highest cell selectivty. An increase in the net charge from 6 to 8 did not result in the improvement of antimicrobial potency. Membrane-simulating experiments showed that the peptides preferentially bound to negatively charged phospholipids over zwitterionic phospholipids, which led to greater cell selectivity. A membrane depolarization assay showed that GLI13-5 killed bacteria by targeting the cyt...Continue Reading

Citations

May 7, 2013·Developmental and Comparative Immunology·Tryntsje CuperusHenk P Haagsman
Oct 16, 2016·BMC Veterinary Research·Mi Ok LeeJames E Womack
Sep 21, 2013·Acta Biochimica Et Biophysica Sinica·Yao GuBaojing Cheng
Oct 26, 2018·Medicinal Research Reviews·Jiajun WangAnshan Shan

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