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

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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

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Publication details

The article was received on 20 Aug 2019, accepted on 27 Oct 2019 and first published on 30 Oct 2019


Article type: Paper
DOI: 10.1039/C9OB01839E
Org. Biomol. Chem., 2019, Advance Article
  • Open access: Creative Commons BY license
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    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, Advance Article , DOI: 10.1039/C9OB01839E

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