Triple helical collagen-like peptides: Engineering and applications in matrix biology

Takaki Koide*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

63 Citations (Scopus)


Collagen, a large insoluble protein with a characteristic triple helical structure, is found as the most prominent component of extracellular matrix. The functions of collagen are not limited to providing mechanical strength to various tissues and organs as a structural protein, as it has been pointed out that collagen exhibits various biological functions through specific interactions with other macromolecules. However, the use of native triple helical collagen is often troublesome because of its insolubility and gelating properties. Instead, triple helical collagen-like peptides have been designed and are used as collagen surrogates in studies on collagen structure, stability, and biological functions including binding to other proteins and cultured cells. This article reviews recent progress in peptide design, synthesis, and the applications of collagen-like peptides in current matrix biology, while emphasizing the advantages of the peptide-based strategy.

Original languageEnglish
Pages (from-to)131-141
Number of pages11
JournalConnective Tissue Research
Issue number3
Publication statusPublished - 2005
Externally publishedYes


  • Collagen
  • Peptides
  • Triple helix

ASJC Scopus subject areas

  • Rheumatology
  • Biochemistry
  • Orthopedics and Sports Medicine
  • Molecular Biology
  • Cell Biology


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