Cyclic Peptides for Efficient Detection of Collagen

Chembiochem. 2018 Aug 6;19(15):1613-1617. doi: 10.1002/cbic.201800166. Epub 2018 Jun 21.


We report here a new class of collagen-binding peptides, cyclic collagen-mimetic peptides (cCMPs), that efficiently hybridize with the triple-helix-forming portions of collagen. cCMPs are composed of two parallel collagen-like (Xaa-Yaa-Gly)n strands with both termini tethered by covalent linkages. Enzyme-linked immunosorbent assays and western blotting analysis showed that cCMPs exhibit more potent affinity toward collagen than reported collagen-binding peptides and can specifically detect different collagen polypeptides in a mixture of proteins. Collagen secreted from cultured cells was detected by confocal microscopy with fluorescein-labeled cCMP. The cCMP is also shown to detect sensitively folding intermediates in the endoplasmic reticulum, something that was difficult to visualize with conventional collagen detectors. Molecular-dynamics simulations suggested that a cCMP forms a more stably hybridized product than its single-chain counterpart; this could explain why cCMP has higher affinity toward denatured collagen. These results indicate the usefulness of cCMPs as tools for detecting denatured collagen.

Keywords: collagen; collagen-mimetic peptide; hybridization; triple helixes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • Cell Line
  • Collagen / analysis*
  • Enzyme-Linked Immunosorbent Assay
  • Fluorescein / chemistry*
  • Fluorescent Dyes / chemistry*
  • Mice
  • Microscopy, Confocal
  • Peptides, Cyclic / chemistry*


  • Fluorescent Dyes
  • Peptides, Cyclic
  • Collagen
  • Fluorescein