Optimization of interstrand interactions enables burn detection with a collagen-mimetic peptide
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c9ob01839e.pdf
Description
Published version
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1.49 MB
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Adobe PDF
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Author(s)
Dones-Monroig, Jesus M.
Tanrikulu, Ismet Caglar
Raines, Ronald T
Date Issued
November 2019
Journal
Organic & biomolecular chemistry
Publisher
Royal Society of Chemistry (RSC)
Citation
Dones, Jesús M. et al. “Optimization of interstrand interactions enables burn detection with a collagen-mimetic peptide.” Organic & biomolecular chemistry, vol. 17, no. 46, 2019, pp.9906-9912 © 2019 The Author(s)
Version
Final published version
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 acomputational screen, we identify (flpHypGly)₇as an optimal monomeric CMP for heterotrimer formation.Wefind that (flpHypGly)₇ forms stable triple helices with (ProProGly)₇ but not with itself. The nonnaturalamino acid HflpOH, which is (2S,4S)-4-fluoroproline, is not toxic to humanfibroblasts or keratinocytes.Conjugation of (flpHypGly)₇ to afluorescent dye enables the facile detection of burned collagenoustissue with high specificity. The ubiquity of collagen and the prevalence of injuries and diseases thatdisrupt endogenous collagen suggests widespread utility for this approach.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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Creative Commons Attribution 3.0 unported license
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DOI of Published Version
https://doi.org/10.1039/c9ob01839e
