Essential but sparse collagen hydroxylysyl post-translational modifications detected by DNP NMR.
Accepted version
Peer-reviewed
Repository URI
Repository DOI
Change log
Authors
Chow, Wing Ying https://orcid.org/0000-0003-0719-5958
Li, Rui
Goldberga, Ieva https://orcid.org/0000-0003-4284-3527
Reid, David G https://orcid.org/0000-0003-2464-5295
Rajan, Rakesh
Abstract
The sparse but functionally essential post-translational collagen modification 5-hydroxylysine can undergo further transformations, including crosslinking, O-glycosylation, and glycation. Dynamic nuclear polarization (DNP) and stable isotope enriched lysine incorporation provide sufficient solid-state NMR sensitivity to identify these adducts directly in skin and vascular smooth muscle cell extracellular matrix (ECM), without extraction procedures, by comparison with chemical shifts of model compounds. Thus, DNP provides access to the elucidation of structural consequences of collagen modifications in intact tissue.
Description
Keywords
0601 Biochemistry and Cell Biology, Basic Science, 1.1 Normal biological development and functioning
Journal Title
Chem Commun (Camb)
Conference Name
Journal ISSN
1359-7345
1364-548X
1364-548X
Volume Title
54
Publisher
Royal Society of Chemistry (RSC)
Publisher DOI
Sponsorship
EPSRC (1652492)
Medical Research Council (MR/M01066X/1)
Biotechnology and Biological Sciences Research Council (BB/G021392/1)
Medical Research Council (MR/M01066X/1)
Biotechnology and Biological Sciences Research Council (BB/G021392/1)