Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance upgrade on Thursday 4th of May 2017 from 8.00am to 9.00am (BST).

During this time our websites will be offline temporarily. If you have any questions please use the feedback button on this page. We apologise for any inconvenience this might cause and thank you for your patience.

Issue 30, 2012
Previous Article Next Article

Peptides that anneal to natural collagen in vitro and ex vivo

Author affiliations


Collagen comprises ¼ of the protein in humans and ¾ of the dry weight of human skin. Here, we implement recent discoveries about the structure and stability of the collagen triple helix to design new chemical modalities that anchor to natural collagen. The key components are collagen mimetic peptides (CMPs) that are incapable of self-assembly into homotrimeric triple helices, but are able to anneal spontaneously to natural collagen. We show that such CMPs containing 4-fluoroproline residues, in particular, bind tightly to mammalian collagen in vitro and to a mouse wound ex vivo. These synthetic peptides, coupled to dyes or growth factors, could herald a new era in assessing or treating wounds.

Graphical abstract: Peptides that anneal to natural collagen in vitro and ex vivo

Back to tab navigation
Please wait while Download options loads

Supplementary files

Publication details

The article was received on 25 Jan 2012, accepted on 21 Mar 2012 and first published on 23 Mar 2012

Article type: Paper
DOI: 10.1039/C2OB25190F
Citation: Org. Biomol. Chem., 2012,10, 5892-5897
  •   Request permissions

    Peptides that anneal to natural collagen in vitro and ex vivo

    S. Chattopadhyay, C. J. Murphy, J. F. McAnulty and R. T. Raines, Org. Biomol. Chem., 2012, 10, 5892
    DOI: 10.1039/C2OB25190F

Search articles by author