In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR

R. Li; R. Rajan; W. C. V. Wong; D. G. Reid; M. J. Duer; V. J. Somovilla; N. Martinez-Saez; G. J. L. Bernardes; R. Hayward; C. M. Shanahan

doi:10.1039/C7CC06624D

In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR†

R. Li,^a R. Rajan,^a W. C. V. Wong,^a D. G. Reid,

^a M. J. Duer,*^a V. J. Somovilla,

‡^a N. Martinez-Saez,‡^a G. J. L. Bernardes,

^a R. Hayward^b and C. M. Shanahan^b

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* Corresponding authors

^a Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
E-mail: mjd13@cam.ac.uk
Fax: +44(0)1223-336362
Tel: +44(0)1223-736394

^b BHF Centre of Research Excellence, Cardiovascular Division, King's College London, London SE5 9NU, UK

Abstract

Non-enzymatic glycation of extracellular matrix with (U-¹³C₅)-D-ribose-5-phosphate (R5P), enables in situ 2D ssNMR identification of many deleterious protein modifications and crosslinks, including previously unreported oxalamido and hemiaminal (CH₃–CH(OH)NHR) substructures. Changes in charged residue proportions and distribution may be as important as crosslinking in provoking and understanding harmful tissue changes.

Chemical Communications

In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR†

Abstract

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In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR

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