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Cyclic Peptide Mimetic of Damaged Collagen
Author(s) -
Aubrey J. Ellison,
I. Caglar Tanrikulu,
Jesús M. Dones,
Ronald T. Raines
Publication year - 2020
Publication title -
biomacromolecules
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.689
H-Index - 220
eISSN - 1526-4602
pISSN - 1525-7797
DOI - 10.1021/acs.biomac.0c00103
Subject(s) - peptide , chemistry , triple helix , in vitro , collagen helix , in vivo , biophysics , duplex (building) , lysine , cyclic peptide , monomer , biochemistry , amino acid , stereochemistry , dna , biology , organic chemistry , polymer , microbiology and biotechnology
Collagen is the most abundant protein in humans and the major component of human skin. Collagen mimetic peptides (CMPs) can anneal to damaged collagen in vitro and in vivo. A duplex of CMPs was envisioned as a macromolecular mimic for damaged collagen. The duplex was synthesized on a solid support from the amino groups of a lysine residue and by using olefin metathesis to link the N termini. The resulting cyclic peptide, which is a monomer in solution, binds to CMPs to form a triple helix. Among these, CMPs that are engineered to avoid the formation of homotrimers but preorganized to adopt the conformation of a collagen strand exhibit enhanced association. Thus, this cyclic peptide enables the assessment of CMPs for utility in annealing to damaged collagen. Such CMPs have potential use in the diagnosis and treatment of fibrotic diseases and wounds.

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