C-Terminal Modifications Broaden Activity of the Proline-Rich Antimicrobial Peptide, Chex1-Arg20

Wenyi Li, Julien Tailhades, M. Akhter Hossain, Neil M. O'Brien-Simpson, Eric C. Reynolds, Laszlo Otvos, Frances Separovic, John D. Wade

Research output: Contribution to journalArticleResearchpeer-review

12 Citations (Scopus)

Abstract

A series of N- and C-terminal modifications of the monomeric proline-rich antimicrobial peptide, Chex1-Arg20, was obtained via different chemical strategies using Fmoc/tBu solid-phase peptide synthesis in order to study their effects on a panel of Gram-negative bacteria. In particular, C-terminal modifications with hydrazide or alcohol functions extended their antibacterial activity from E. coli and K. pneumoniae to other Gram-negative species, A. baumannii and P. aeruginosa. Furthermore, these analogues did not show cytotoxicity towards mammalian cells. Hence, such modifications may aid in the development of more potent proline-rich antimicrobial peptides with a greater spectrum of activity against Gram-negative bacteria than the parent peptide.

Original languageEnglish
Pages (from-to)1373-1378
Number of pages6
JournalAustralian Journal of Chemistry
Volume68
Issue number9
DOIs
Publication statusPublished - 12 Jun 2015
Externally publishedYes

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