Peptides that anneal to natural collagen in vitro and ex vivo

Sayani Chattopadhyay, Christopher J Murphy, Jonathan F. McAnulty, Ronald T. Raines

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


Collagen comprises of the protein in humans and 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.

Original languageEnglish (US)
Pages (from-to)5892-5897
Number of pages6
JournalOrganic and Biomolecular Chemistry
Issue number30
StatePublished - Aug 14 2012

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Biochemistry


Dive into the research topics of 'Peptides that anneal to natural collagen in vitro and ex vivo'. Together they form a unique fingerprint.

Cite this