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, 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

^*Corresponding author for this work

Cardiovascular Sciences

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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.

Original language	English
Pages (from-to)	13316-13319
Number of pages	4
Journal	Chemical communications (Cambridge, England)
Volume	53
Issue number	100
Early online date	1 Dec 2017
DOIs	https://doi.org/10.1039/c7cc06624d
Publication status	E-pub ahead of print - 1 Dec 2017

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10.1039/c7cc06624dLicence: CC BY

In situ characterization of_LI_1December2017_GOLD VoR (CC BY)Final published version, 1.83 MBLicence: CC BY

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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. (2017). In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR. Chemical communications (Cambridge, England), 53(100), 13316-13319. Advance online publication. https://doi.org/10.1039/c7cc06624d

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title = "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.",

author = "R. Li and R. Rajan and Wong, {W. C.V.} and Reid, {D. G.} and Duer, {M. J.} and Somovilla, {V. J.} and N. Martinez-Saez and Bernardes, {G. J.L.} and R. Hayward and Shanahan, {C. M.}",

year = "2017",

month = dec,

day = "1",

doi = "10.1039/c7cc06624d",

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Li, R, Rajan, R, Wong, WCV, Reid, DG, Duer, MJ, Somovilla, VJ, Martinez-Saez, N, Bernardes, GJL, Hayward, R & Shanahan, CM 2017, 'In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR', Chemical communications (Cambridge, England), vol. 53, no. 100, pp. 13316-13319. https://doi.org/10.1039/c7cc06624d

TY - JOUR

T1 - In situ characterization of advanced glycation end products (AGEs) in collagen and model extracellular matrix by solid state NMR

AU - Li, R.

AU - Rajan, R.

AU - Wong, W. C.V.

AU - Reid, D. G.

AU - Duer, M. J.

AU - Somovilla, V. J.

AU - Martinez-Saez, N.

AU - Bernardes, G. J.L.

AU - Hayward, R.

AU - Shanahan, C. M.

PY - 2017/12/1

Y1 - 2017/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85038420545&partnerID=8YFLogxK

U2 - 10.1039/c7cc06624d

DO - 10.1039/c7cc06624d

M3 - Article

AN - SCOPUS:85038420545

SN - 1359-7345

VL - 53

SP - 13316

EP - 13319

JO - Chemical communications (Cambridge, England)

JF - Chemical communications (Cambridge, England)

IS - 100

ER -

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

Abstract

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