Essential but sparse collagen hydroxylysyl post-translational modifications detected by DNP NMR

被引：11

作者：

Chow, Wing Ying ^{[1
]}

Li, Rui ^{[2
]}

Goldberga, Ieva ^{[2
]}

Reid, David G. ^{[2
]}

Rajan, Rakesh ^{[2
]}

Clark, Jonathan ^{[3
]}

Oschkinat, Hartmut ^{[1
]}

Duer, Melinda J. ^{[2
]}

Hayward, Robert ^{[4
]}

Shanahan, Catherine M. ^{[4
]}

机构：

[1] Leibniz Forschungsinst Mol Pharmakol, Campus Buch,Robert Roessle Str 10, D-13125 Berlin, Germany

[2] Univ Cambridge, Dept Chem, Lensfield Rd, Cambridge CB2 1EW, England

[3] Babraham Inst, Babraham Res Campus, Cambridge CB22 3AT, England

[4] Kings Coll London, BHF Ctr Res Excellence, Cardiovasc Div, London SE5 9NU, England

来源：

CHEMICAL COMMUNICATIONS | 2018年 / 54卷 / 89期

基金：

英国生物技术与生命科学研究理事会; 英国工程与自然科学研究理事会; 英国医学研究理事会; 欧盟地平线“2020”;

关键词：

DYNAMIC-NUCLEAR-POLARIZATION; SOLID-STATE NMR; GLU-GAL-HYL; CROSS-LINKING; EXTRACELLULAR-MATRIX; STRUCTURAL-ANALYSIS; SKIN COLLAGEN; END-PRODUCTS; I COLLAGEN; MAS NMR;

D O I：

10.1039/c8cc04960b

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The sparse but functionally essential post-translational collagen modification 5-hydroxylysine can undergo further transformations, including crosslinking, O-glycosylation, and glycation. Dynamic nuclear polarization (DNP) and stable isotope enriched lysine incorporation provide sufficient solid-state NMR sensitivity to identify these adducts directly in skin and vascular smooth muscle cell extracellular matrix (ECM), without extraction procedures, by comparison with chemical shifts of model compounds. Thus, DNP provides access to the elucidation of structural consequences of collagen modifications in intact tissue.

引用

页码：12570 / 12573

页数：4

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