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Cyclic Peptide Mimetic of Damaged Collagen
[Image: see text] 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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7192010/ https://www.ncbi.nlm.nih.gov/pubmed/32159956 http://dx.doi.org/10.1021/acs.biomac.0c00103 |
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author | Ellison, Aubrey J. Tanrikulu, I. Caglar Dones, Jesús M. Raines, Ronald T. |
author_facet | Ellison, Aubrey J. Tanrikulu, I. Caglar Dones, Jesús M. Raines, Ronald T. |
author_sort | Ellison, Aubrey J. |
collection | PubMed |
description | [Image: see text] 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. |
format | Online Article Text |
id | pubmed-7192010 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-71920102020-04-30 Cyclic Peptide Mimetic of Damaged Collagen Ellison, Aubrey J. Tanrikulu, I. Caglar Dones, Jesús M. Raines, Ronald T. Biomacromolecules [Image: see text] 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. American Chemical Society 2020-03-11 2020-04-13 /pmc/articles/PMC7192010/ /pubmed/32159956 http://dx.doi.org/10.1021/acs.biomac.0c00103 Text en Copyright © 2020 American Chemical Society This is an open access article published under a Creative Commons Attribution (CC-BY) License (http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html) , which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited. |
spellingShingle | Ellison, Aubrey J. Tanrikulu, I. Caglar Dones, Jesús M. Raines, Ronald T. Cyclic Peptide Mimetic of Damaged Collagen |
title | Cyclic Peptide
Mimetic of Damaged Collagen |
title_full | Cyclic Peptide
Mimetic of Damaged Collagen |
title_fullStr | Cyclic Peptide
Mimetic of Damaged Collagen |
title_full_unstemmed | Cyclic Peptide
Mimetic of Damaged Collagen |
title_short | Cyclic Peptide
Mimetic of Damaged Collagen |
title_sort | cyclic peptide
mimetic of damaged collagen |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7192010/ https://www.ncbi.nlm.nih.gov/pubmed/32159956 http://dx.doi.org/10.1021/acs.biomac.0c00103 |
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