Peptidic “Molecular Beacon” for Collagen
Name
nihms-2034974.pdf
Description
Accepted version
Size
1.21 MB
Format
Adobe PDF
Checksum (MD5)
d4572a0256fd705e39931b65884ef4f3
Author(s)
Yang, Jinyi
Quan, Yifan
Ouyang, Yifu
Tan, Kong Ooi
Weber, Ralph T
Griffin, Robert G
Raines, Ronald T
Date Issued
September 3, 2024
Journal
Biomacromolecules
Publisher
American Chemical Society
Citation
Peptidic “Molecular Beacon” for Collagen. Jinyi Yang, Yifan Quan, Yifu Ouyang, Kong Ooi Tan, Ralph T. Weber, Robert G. Griffin, and Ronald T. Raines. Biomacromolecules 2024 25 (10), 6773-6779.
Version
Author's final manuscript
Abstract
Collagen-mimetic peptides (CMP) have been invaluable tools for understanding the structure and function of collagen, which is the most abundant protein in animals. CMPs have also been developed as probes that detect damaged collagen because of the specificity required to form a collagen triple helix. These probes are not, however, ratiometric. Here, we used EPR spectroscopy to determine the end-to-end distances of CMPs that do not form stable homotrimeric helices. We found that those distances are shorter than the distances in the context of a collagen triple helix, suggesting their potential utility as a “molecular beacon” and guiding the choice and location of a pendant fluorophore–quencher pair. We then showed that a molecular beacon based on a glycine–(2S,4S)-4-fluoroproline–(2S,4R)-4-hydroxyproline tripeptide repeat and EDANS–DABCYL pair enabled the ratiometric detection of its binding to both other CMPs and natural mammalian collagen. These results provide guidance for the development of a new modality for detecting damaged collagen in physiological settings.
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1021/acs.biomac.4c01000
