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Molecules 2018, 23(9), 2314; https://doi.org/10.3390/molecules23092314

Glycosaminoglycan-Protein Interactions by Nuclear Magnetic Resonance (NMR) Spectroscopy

1,* and 2,*
1
Department of BioMolecular Sciences, Division of Pharmacognosy and Research Institute of Pharmaceutical Sciences, School of Pharmacy, University of Mississippi, Oxford, MS 38677-1848, USA
2
School of Molecular Sciences, Arizona State University, Tempe, AZ 85287-0112, USA
*
Authors to whom correspondence should be addressed.
Received: 8 August 2018 / Revised: 29 August 2018 / Accepted: 5 September 2018 / Published: 11 September 2018
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Abstract

Nuclear magnetic resonance (NMR) spectroscopy is one of the most utilized and informative analytical techniques for investigating glycosaminoglycan (GAG)-protein complexes. NMR methods that are commonly applied to GAG-protein systems include chemical shift perturbation, saturation transfer difference, and transferred nuclear Overhauser effect. Although these NMR methods have revealed valuable insight into the protein-GAG complexes, elucidating high-resolution structural and dynamic information of these often transient interactions remains challenging. In addition, preparation of structurally homogeneous and isotopically enriched GAG ligands for structural investigations continues to be laborious. As a result, understanding of the structure-activity relationship of GAGs is still primitive. To overcome these deficiencies, several innovative NMR techniques have been developed lately. Here, we review some of the commonly used techniques along with more novel methods such as waterLOGSY and experiments to examine structure and dynamic of lysine and arginine side chains to identify GAG-binding sites. We will also present the latest technology that is used to produce isotopically enriched as well as paramagnetically tagged GAG ligands. Recent results that were obtained from solid-state NMR of amyloid’s interaction with GAG are also presented together with a brief discussion on computer assisted modeling of GAG-protein complexes using sparse experimental data. View Full-Text
Keywords: glycosaminoglycan; GAG binding site; GAG-protein interactions; isotopic labeling; NMR; paramagnetic labeling glycosaminoglycan; GAG binding site; GAG-protein interactions; isotopic labeling; NMR; paramagnetic labeling
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
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Pomin, V.H.; Wang, X. Glycosaminoglycan-Protein Interactions by Nuclear Magnetic Resonance (NMR) Spectroscopy. Molecules 2018, 23, 2314.

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