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

Non-enzymatic glycation of extracellular matrix with (U-(13)C(5))-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(3)–CH(OH)NHR) substructures. Changes in charged...

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Detalles Bibliográficos
Autores principales: Li, R., Rajan, R., Wong, W. C. V., Reid, D. G., Duer, M. J., Somovilla, V. J., Martinez-Saez, N., Bernardes, G. J. L., Hayward, R., Shanahan, C. M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2017
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5774432/
https://www.ncbi.nlm.nih.gov/pubmed/29192920
http://dx.doi.org/10.1039/c7cc06624d
Descripción
Sumario:Non-enzymatic glycation of extracellular matrix with (U-(13)C(5))-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(3)–CH(OH)NHR) substructures. Changes in charged residue proportions and distribution may be as important as crosslinking in provoking and understanding harmful tissue changes.

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