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

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.

SUBMITTER: Li R 

PROVIDER: S-EPMC5774432 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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

Li R R   Rajan R R   Wong W C V WCV   Reid D G DG   Duer M J MJ   Somovilla V J VJ   Martinez-Saez N N   Bernardes G J L GJL   Hayward R R   Shanahan C M CM  

Chemical communications (Cambridge, England) 20171201 100

Non-enzymatic glycation of extracellular matrix with (U-<sup>13</sup>C<sub>5</sub>)-d-ribose-5-phosphate (R5P), enables in situ 2D ssNMR identification of many deleterious protein modifications and crosslinks, including previously unreported oxalamido and hemiaminal (CH<sub>3</sub>-CH(OH)NHR) substructures. Changes in charged residue proportions and distribution may be as important as crosslinking in provoking and understanding harmful tissue changes. ...[more]

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