In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR-Reference-Cited by-同舟云学术

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

Published:2017 Issue:100 Volume:53 Page:13316-13319
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Li R.¹²³⁴,Rajan R.¹²³⁴,Wong W. C. V.¹²³⁴,Reid D. G.¹²³⁴^ORCID,Duer M. J.¹²³⁴,Somovilla V. J.¹²³⁴^ORCID,Martinez-Saez N.¹²³⁴,Bernardes G. J. L.¹²³⁴^ORCID,Hayward R.⁵⁶⁷⁸⁴,Shanahan C. M.⁵⁶⁷⁸⁴

Affiliation:

1. Department of Chemistry

2. University of Cambridge

3. Cambridge CB2 1EW

4. UK

5. BHF Centre of Research Excellence

6. Cardiovascular Division

7. King's College London

8. London SE5 9NU

Abstract

Pathological glycation of extracellular matrix modelled with ¹³C-labelled sugars yields unique novel atomic level NMR structural and chemical insights non-destructively.

Funder

Medical Research Council

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2017/CC/C7CC06624D

Reference30 articles.

1. Conversion of Arginine into Ornithine by Advanced Glycation in Senescent Human Collagen and Lens Crystallins

2. Induction of advanced glycation end products and alterations of the tensile properties of articular cartilage

3. Cross-Linking in Collagen by Nonenzymatic Glycation Increases the Matrix Stiffness in Rabbit Achilles Tendon

4. Influence of nonenzymatic glycation on biomechanical properties of cortical bone

5. Methylglyoxal Inhibits the Binding Step of Collagen Phagocytosis

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