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 journalArticle

17 Citations (Scopus)

Abstract

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
Volume10
Issue number30
DOIs
StatePublished - Aug 14 2012

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collagens
peptides
Collagen
Peptides
helices
Wounds and Injuries
In Vitro Techniques
Anchors
Self assembly
mice
self assembly
Intercellular Signaling Peptides and Proteins
Skin
Coloring Agents
dyes
proteins
Weights and Measures
Proteins

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Biochemistry

Cite this

Peptides that anneal to natural collagen in vitro and ex vivo. / Chattopadhyay, Sayani; Murphy, Christopher J; McAnulty, Jonathan F.; Raines, Ronald T.

In: Organic and Biomolecular Chemistry, Vol. 10, No. 30, 14.08.2012, p. 5892-5897.

Research output: Contribution to journalArticle

Chattopadhyay, Sayani ; Murphy, Christopher J ; McAnulty, Jonathan F. ; Raines, Ronald T. / Peptides that anneal to natural collagen in vitro and ex vivo. In: Organic and Biomolecular Chemistry. 2012 ; Vol. 10, No. 30. pp. 5892-5897.
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