Glycosaminoglycan-protein interactions by nuclear magnetic resonance (NMR) spectroscopy

Vitor H. Pomin, Xu Wang

Research output: Contribution to journalReview article

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.

Original languageEnglish (US)
Article number2314
JournalMolecules
Volume23
Issue number9
DOIs
StatePublished - Sep 11 2018

Fingerprint

magnetic resonance spectroscopy
Glycosaminoglycans
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
proteins
nuclear magnetic resonance
Proteins
Nuclear magnetic resonance
interactions
Overhauser effect
ligands
lysine
chemical equilibrium
Ligands
Chemical shift
solid state
saturation
Structure-Activity Relationship
perturbation
preparation

Keywords

  • GAG binding site
  • GAG-protein interactions
  • Glycosaminoglycan
  • Isotopic labeling
  • NMR
  • Paramagnetic labeling

ASJC Scopus subject areas

  • Analytical Chemistry
  • Chemistry (miscellaneous)
  • Molecular Medicine
  • Pharmaceutical Science
  • Drug Discovery
  • Physical and Theoretical Chemistry
  • Organic Chemistry

Cite this

Glycosaminoglycan-protein interactions by nuclear magnetic resonance (NMR) spectroscopy. / Pomin, Vitor H.; Wang, Xu.

In: Molecules, Vol. 23, No. 9, 2314, 11.09.2018.

Research output: Contribution to journalReview article

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