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 language | English (US) |
|---|---|
| Pages (from-to) | 5892-5897 |
| Number of pages | 6 |
| Journal | Organic and Biomolecular Chemistry |
| Volume | 10 |
| Issue number | 30 |
| DOIs | |
| State | Published - Aug 14 2012 |
Fingerprint
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 journal › Article
}
TY - JOUR
T1 - Peptides that anneal to natural collagen in vitro and ex vivo
AU - Chattopadhyay, Sayani
AU - Murphy, Christopher J
AU - McAnulty, Jonathan F.
AU - Raines, Ronald T.
PY - 2012/8/14
Y1 - 2012/8/14
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84863948648&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84863948648&partnerID=8YFLogxK
U2 - 10.1039/c2ob25190f
DO - 10.1039/c2ob25190f
M3 - Article
C2 - 22522497
AN - SCOPUS:84863948648
VL - 10
SP - 5892
EP - 5897
JO - Organic and Biomolecular Chemistry
JF - Organic and Biomolecular Chemistry
SN - 1477-0520
IS - 30
ER -