AI Article Synopsis
- The post-translational modification of collagen, specifically 5-hydroxylysine, is crucial for its function and can lead to various transformations like crosslinking and glycosylation.
- Dynamic nuclear polarization (DNP) techniques, along with isotope labeling, enhance NMR sensitivity, allowing direct identification of these modifications in tissue samples like skin and vascular smooth muscle without needing extraction.
- This approach enables researchers to better understand how collagen modifications affect its structure in living tissues.
Article Abstract
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.
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| http://dx.doi.org/10.1039/c8cc04960b | DOI Listing |
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