Related ArticlesGalectin-Glycan Interactions: Guidelines for Monitoring by 77 Se NMR Spectroscopy, and Solvent (H2 O/D2 O) Impact on Binding.
Chemistry. 2021 Jan 04;27(1):316-325
Authors: Diercks T, Medrano FJ, FitzGerald FG, Beckwith D, Pedersen MJ, Reihill M, Ludwig AK, Romero A, Oscarson S, Cudic M, Gabius HJ
Abstract
Functional pairing between cellular glycoconjugates and tissue lectins like galectins has wide (patho)physiological significance. Their study is facilitated by nonhydrolysable derivatives of the natural O-glycans, such as S- and Se-glycosides. The latter enable extensive analyses by specific 77 Se NMR spectroscopy, but still remain underexplored. By using the example of selenodigalactoside (SeDG) and the human galectin-1 and -3, we have evaluated diverse 77 Se NMR detection methods and propose selective 1 H,77 Se heteronuclear Hartmann-Hahn transfer for efficient use in competitive NMR screening against a selenoglycoside spy ligand. By fluorescence anisotropy, circular dichroism, and isothermal titration calorimetry (ITC), we show that the affinity and thermodynamics of SeDG binding by galectins are similar to thiodigalactoside (TDG) and N-acetyllactosamine (LacNAc), confirming that Se substitution has no major impact. ITC data in D2 O versus H2 O are similar for TDG and LacNAc binding by both galectins, but a solvent effect, indicating solvent rearrangement at the binding site, is hinted at for SeDG and clearly observed for LacNAc dimers with extended chain length.
Glycan-Protein Interactions in NMDA Receptors Revealed with Computational Modeling and NMR Spectroscopy
Glycan-Protein Interactions in NMDA Receptors Revealed with Computational Modeling and NMR Spectroscopy
Publication date: 2 February 2018
Source:Biophysical Journal, Volume 114, Issue 3, Supplement 1</br>
Author(s): Anton V. Sinitskiy, Ganesh P. Subedi, Adam W. Barb, Vijay S. Pande</br>
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02-07-2018 03:41 PM
[NMR paper] Protein-Glycan Quinary Interactions in Crowding Environment Unveiled by NMR Spectroscopy.
Protein-Glycan Quinary Interactions in Crowding Environment Unveiled by NMR Spectroscopy.
Related Articles Protein-Glycan Quinary Interactions in Crowding Environment Unveiled by NMR Spectroscopy.
Chemistry. 2017 Jun 25;:
Authors: Diniz A, S Dias J, Jiménez-Barbero J, Marcelo F, Cabrita EJ
Abstract
Protein-glycan interactions as modulators for quinary structure in crowding environments were explored. The interaction between human galectin 3 (Gal-3) and distinct macromolecular crowders, such as bovine and human serum albumin (BSA...
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06-27-2017 05:28 PM
[NMR paper] Monitoring the Interactions of a Ternary Complex Using NMR Spectroscopy: The Case of Sugars, Polyphenols, and Proteins.
Monitoring the Interactions of a Ternary Complex Using NMR Spectroscopy: The Case of Sugars, Polyphenols, and Proteins.
Monitoring the Interactions of a Ternary Complex Using NMR Spectroscopy: The Case of Sugars, Polyphenols, and Proteins.
Anal Chem. 2016 Dec 20;88(24):12470-12478
Authors: Faurie B, Dufourc EJ, Laguerre M, Pianet I
Abstract
Gaining insight into intermolecular interactions between multiple species is possible at an atomic level by looking at different parameters using different NMR techniques. In the specific...
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02-15-2017 03:40 PM
[NMR paper] Intra- and inter-molecular interactions of human galectin-3: assessment by full-assignment-based NMR.
Intra- and inter-molecular interactions of human galectin-3: assessment by full-assignment-based NMR.
Related Articles Intra- and inter-molecular interactions of human galectin-3: assessment by full-assignment-based NMR.
Glycobiology. 2016 Feb 23;
Authors: Ippel H, Miller MC, Vértesy S, Zhang Y, Cañada FJ, Suylen D, Umemoto K, Romanò C, Hackeng T, Tai G, Leffler H, Kopitz J, André S, Kübler D, Jiménez-Barbero J, Oscarson S, Gabius HJ, Mayo KH
Abstract
Galectin-3 is an adhesion/growth-regulatory protein with a modular design...
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02-27-2016 12:52 AM
[NMR paper] NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
Related Articles NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
Adv Exp Med Biol. 2015;870:49-122
Authors: Brutscher B, Felli IC, Gil-Caballero S, Hošek T, Kümmerle R, Piai A, Pierattelli R, Sólyom Z
Abstract
Thanks to recent improvements in NMR instrumentation, pulse sequence design, and...
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09-21-2015 03:01 PM
[NMR paper] Monitoring Glycan-Protein Interactions by NMR Spectroscopic Analysis: A Simple Chemical Tag That Mimics Natural CH-? Interactions.
Monitoring Glycan-Protein Interactions by NMR Spectroscopic Analysis: A Simple Chemical Tag That Mimics Natural CH-? Interactions.
Related Articles Monitoring Glycan-Protein Interactions by NMR Spectroscopic Analysis: A Simple Chemical Tag That Mimics Natural CH-? Interactions.
Chemistry. 2015 Jul 14;
Authors: Calle LP, Echeverria B, Franconetti A, Serna S, Fernández-Alonso MC, Diercks T, Cañada FJ, Ardá A, Reichardt NC, Jiménez-Barbero J
Abstract
Detection of molecular recognition processes requires robust, specific, and easily...
[NMR paper] Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Chemistry. 2013 Feb 28;
Authors: Matei E, André S, Glinschert A, Infantino AS, Oscarson S, Gabius HJ, Gronenborn AM
Abstract
NMR spectroscopy and isothermal titration calorimetry (ITC) are powerful methods to investigate ligand-protein interactions. Here, we present a versatile and sensitive fluorine NMR...