Collagen-like antimicrobial peptides

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

Research output: Contribution to journalArticlepeer-review

6 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 - Nov 4 2016


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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry


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