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

Ryo Masuda, Yui Dazai, Takehiko Mima, Takaki Koide

    Research output: Contribution to journalArticle

    2 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 - 2017 Jan 1

    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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