Structure–activity relationships and action mechanisms of collagen-like antimicrobial peptides

Ryo Masuda, Yui Dazai, Takehiko Mima, Takaki Koide

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

An antimicrobial triple-helical peptide, R3, was previously obtained from a collagen-like combinatorial peptide library. In this research, based on structure–activity relationship studies of R3, a more potent peptide, RR4, with increased positive net charge and charge density relative to R3, was developed. RR4 exhibited antimicrobial activity against both Gram-negative and Gram-positive bacterial strains, including multidrug-resistant strains. Its action could be attributed to entry into cells and interactions with intercellular molecules such as DNA/RNA that inhibited cell division rather than increasing bacterial membrane permeability. Furthermore, RR4 exhibited remarkable stability in serum and low cytotoxicity.

Original languageEnglish
Article numbere22931
JournalBiopolymers
Volume108
Issue number1
DOIs
Publication statusPublished - Jan 1 2017

Fingerprint

Collagen
Peptides
Peptide Library
Specific Gravity
Cytotoxicity
Charge density
Cell Communication
Cell Division
Permeability
Cells
RNA
Membranes
Molecules
DNA
Serum
Research

Keywords

  • antimicrobial peptide
  • collagen
  • structure–activity relationship
  • triple helix

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

Cite this

Structure–activity relationships and action mechanisms of collagen-like antimicrobial peptides. / Masuda, Ryo; Dazai, Yui; Mima, Takehiko; Koide, Takaki.

In: Biopolymers, Vol. 108, No. 1, e22931, 01.01.2017.

Research output: Contribution to journalArticle

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