Issue 46, 2019

Optimization of interstrand interactions enables burn detection with a collagen-mimetic peptide

Abstract

Collagen is an abundant component of the extracellular matrix and connective tissues. Some collagen-mimetic peptides (CMPs) that do not form homotrimers can anneal to damaged tissue. Here, through a computational screen, we identify (flpHypGly)7 as an optimal monomeric CMP for heterotrimer formation. We find that (flpHypGly)7 forms stable triple helices with (ProProGly)7 but not with itself. The nonnatural amino acid HflpOH, which is (2S,4S)-4-fluoroproline, is not toxic to human fibroblasts or keratinocytes. Conjugation of (flpHypGly)7 to a fluorescent dye enables the facile detection of burned collagenous tissue with high specificity. The ubiquity of collagen and the prevalence of injuries and diseases that disrupt endogenous collagen suggests widespread utility for this approach.

Graphical abstract: Optimization of interstrand interactions enables burn detection with a collagen-mimetic peptide

Supplementary files

Article information

Article type
Paper
Submitted
20 Aug 2019
Accepted
27 Oct 2019
First published
30 Oct 2019
This article is Open Access
Creative Commons BY license

Org. Biomol. Chem., 2019,17, 9906-9912

Optimization of interstrand interactions enables burn detection with a collagen-mimetic peptide

J. M. Dones, I. C. Tanrikulu, J. V. Chacko, A. B. Schroeder, T. T. Hoang, A. L. F. Gibson, K. W. Eliceiri and R. T. Raines, Org. Biomol. Chem., 2019, 17, 9906 DOI: 10.1039/C9OB01839E

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