Collagen-like antimicrobial peptides

Ryo Masuda, Masakazu Kudo, Yui Dazai, Takehiko Mima, Takaki Koide

    Research output: Contribution to journalArticle

    2 Citations (Scopus)


    Combinatorial library composed of rigid rod-like peptides with a triple-helical scaffold was constructed. The component peptides were designed to have various combinations of basic and neutral (or hydrophobic) amino acid residues based on collagen-like (Gly-Pro-Yaa)-repeating sequences, inspired from the basic and amphiphilic nature of naturally occurring antimicrobial peptides. Screening of the peptide pools resulted in identification of antimicrobial peptides. A structure-activity relationship study revealed that the position of Arg-cluster at N-terminus and cystine knots at C-terminus in the triple helix significantly contributed to the antimicrobial activity. The most potent peptide RO-A showed activity against Gram-negative Escherichia coli and Gram-positive Bacillus subtilis. In addition, Escherichia coli exposed to RO-A resulted in abnormal elongation of the cells. RO-A was also shown to have remarkable stability in human serum and low cytotoxicity to mammalian cells.

    Original languageEnglish
    Pages (from-to)453-459
    Number of pages7
    Publication statusPublished - 2016 Nov 4


    • antimicrobial peptide
    • collagen
    • combinatorial library
    • structure-activity relationship
    • triple helix

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Biomaterials
    • Organic Chemistry

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