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Chem Commun (Camb). 2018 Nov 6;54(89):12570-12573. doi: 10.1039/c8cc04960b.

Essential but sparse collagen hydroxylysyl post-translational modifications detected by DNP NMR.

Author information

1
Leibniz Forschungsinstitut für Molekulare Pharmakologie, Campus Buch, Robert-Roessle Str. 10, Berlin 13125, Germany. oschkinat@fmp-berlin.de.
2
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. mjd13@cam.ac.uk.
3
Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
4
BHF Centre of Research Excellence, Cardiovascular Division, King's College London, London SE5 9NU, UK.

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.

PMID:
30299444
DOI:
10.1039/c8cc04960b

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