Glycans are ubiquitous in nature, decorating our cells and serving as the initial points of contact with any visiting entities. These glycan interactions are fundamental to host-pathogen recognition and are related to various diseases, including inflammation and cancer. Therefore, understanding the conformations and dynamics of glycans, as well as the key features that regulate their interactions with proteins, is crucial for designing new therapeutics. Due to the intrinsic flexibility of...
[NMR paper] Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
The interactions of glycans with proteins modulate many events related to health and disease. In fact, the establishment of these recognition events and their biological consequences are intimately related to the three-dimensional structures of both partners, as well as to their dynamic features and their presentation on the corresponding cell compartments. NMR techniques are unique to disentangle these characteristics and, indeed, diverse NMR-based methodologies have been developed and applied...
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06-03-2024 04:41 PM
[NMR paper] (77)Se-Enriched Selenoglycoside Enables Significant Enhancement in NMR Spectroscopic Monitoring of Glycan-Protein Interactions
(77)Se-Enriched Selenoglycoside Enables Significant Enhancement in NMR Spectroscopic Monitoring of Glycan-Protein Interactions
Detailed investigation of ligand-protein interactions is essential for better understanding of biological processes at the molecular level. Among these binding interactions, the recognition of glycans by lectins is of particular importance in several diseases, such as cancer; therefore, inhibition of glycan-lectin/galectin interactions represents a promising perspective towards developing therapeutics controlling cancer development. The recent introduction of...
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01-22-2022 02:38 AM
[NMR paper] Automated glycan assembly of 19F labelled glycan probes enables high-throughput NMR studies of protein-glycan interactions
Automated glycan assembly of 19F labelled glycan probes enables high-throughput NMR studies of protein-glycan interactions
Protein-glycan interactions mediate important biological processes, including pathogen host invasion and cellular communication. Major challenges to monitoring these low affinity interactions are the required high sensitivity of a biophysical assay and to cover a breath of synthetic well-defined structures. Here, we showcase an expedite approach that integrates automated glycan assembly (AGA) of 19 F labelled probes and high-throughput NMR methods, enabling the study...
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03-30-2021 11:12 PM
[NMR paper] Galectin-Glycan Interactions: Guidelines for Monitoring by 77 Se NMR Spectroscopy, and Solvent (H2 O/D2 O) Impact on Binding.
Galectin-Glycan Interactions: Guidelines for Monitoring by 77 Se NMR Spectroscopy, and Solvent (H2 O/D2 O) Impact on Binding.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.png Related Articles Galectin-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
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02-18-2021 03:17 PM
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 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...
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07-17-2015 03:02 PM
[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...
NMR investigations of glycan conformation, dynamics, and interactions
Linear Mode
