Saturation-Transfer Difference (STD) NMR: A Simple and Fast Method for Ligand Screening and Characterization of Protein Binding

2011 ◽  
Vol 88 (7) ◽  
pp. 990-994 ◽  
Author(s):  
Aldino Viegas ◽  
João Manso ◽  
Franklin L. Nobrega ◽  
Eurico J. Cabrita
Keyword(s):  
Protein Binding ◽  
Fast Method ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Ligand Screening ◽  
Std Nmr

Saturation Transfer Difference (STD) NMR Spectroscopy Characterization of Dual Binding Mode of a Mannose Disaccharide to DC-SIGN

ChemBioChem ◽  
2008 ◽  
Vol 9 (14) ◽  
pp. 2225-2227 ◽  
Author(s):  
Jesús Angulo ◽  
Irene Díaz ◽  
José J. Reina ◽  
Georges Tabarani ◽  
Franck Fieschi ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Binding Mode ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Std Nmr

scholarly journals Investigating the interaction mechanism of fluorescent whitening agents to human serum albumin using saturation transfer difference-NMR, multi-spectroscopy, and docking studies

RSC Advances ◽  
2017 ◽  
Vol 7 (44) ◽  
pp. 27796-27806 ◽  
Author(s):  
Ludan Zhao ◽  
Jiuyang Liu ◽  
Ronghui Guo ◽  
Qiaomei Sun ◽  
Hongqin Yang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Interaction Mechanism ◽  
Docking Studies ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Fluorescent Whitening Agents ◽  
Std Nmr

Characterization of the interaction between two fluorescent whitening agents and human serum albumin: 1H STD-NMR, multi-spectroscopy, and docking studies.

Characterization of heparin–protein interaction by saturation transfer difference (STD) NMR

2014 ◽  
Vol 406 (13) ◽  
pp. 3079-3089 ◽  
Author(s):  
Fei Yu ◽  
Sucharita Roy ◽  
Enrique Arevalo ◽  
John Schaeck ◽  
Jason Wang ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Std Nmr

scholarly journals Multifrequency STD NMR Unveils the Interactions of Antibiotics With Burkholderia multivorans Biofilm Exopolysaccharide

2021 ◽  
Vol 8 ◽  
Author(s):  
Ridvan Nepravishta ◽  
Serena Monaco ◽  
Marco Distefano ◽  
Roberto Rizzo ◽  
Paola Cescutti ◽  
...  
Keyword(s):  
Active Role ◽  
Atomic Level ◽  
Bacterial Cells ◽  
Saturation Transfer ◽  
Burkholderia Multivorans ◽  
Powerful Technique ◽  
Macromolecular Assemblies ◽  
Saturation Transfer Difference ◽  
Std Nmr

Biofilms confine bacterial cells within self-produced matrices, offering advantages such as protection from antibiotics and entrapment of nutrients. Polysaccharides are major components in these macromolecular assemblies, and their interactions with other chemicals are of high relevance for the benefits provided by the biofilm 3D molecular matrix. NMR is a powerful technique for the study and characterization of the interactions between molecules of biological relevance. In this study, we have applied multifrequency saturation transfer difference (STD) NMR and DOSY NMR approaches to elucidate the interactions between the exopolysaccharide produced by Burkholderia multivorans C1576 (EpolC1576) and the antibiotics kanamycin and ceftadizime. The NMR strategies presented here allowed for an extensive characterization at an atomic level of the mechanisms behind the implication of the EpolC1576 in the recalcitrance phenomena, which is the ability of bacteria in biofilms to survive in the presence of antibiotics. Our results suggest an active role for EpolC1576 in the recalcitrance mechanisms toward kanamycin and ceftadizime, though through two different mechanisms.

scholarly journals Saturation transfer difference NMR on the integral trimeric membrane transport protein GltPh determines cooperative substrate binding

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Jenny L. Hall ◽  
Azmat Sohail ◽  
Eurico J. Cabrita ◽  
Colin Macdonald ◽  
Thomas Stockner ◽  
...  
Keyword(s):  
Membrane Transport ◽  
Excitatory Amino Acid ◽  
Transport Protein ◽  
Amino Acid Transporters ◽  
Binding Affinities ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Membrane Transport Protein ◽  
The Central Nervous System ◽  
Std Nmr

Abstract Saturation-transfer difference (STD) NMR spectroscopy is a fast and versatile method which can be applied for drug-screening purposes, allowing the determination of essential ligand binding affinities (KD). Although widely employed to study soluble proteins, its use remains negligible for membrane proteins. Here the use of STD NMR for KD determination is demonstrated for two competing substrates with very different binding affinities (low nanomolar to millimolar) for an integral membrane transport protein in both detergent-solubilised micelles and reconstituted proteoliposomes. GltPh, a homotrimeric aspartate transporter from Pyrococcus horikoshii, is an archaeal homolog of mammalian membrane transport proteins—known as excitatory amino acid transporters (EAATs). They are found within the central nervous system and are responsible for fast uptake of the neurotransmitter glutamate, essential for neuronal function. Differences in both KD’s and cooperativity are observed between detergent micelles and proteoliposomes, the physiological implications of which are discussed.

scholarly journals Saturation Transfer Difference in Characterization of Glycosaminoglycan-Protein Interactions

2020 ◽  
Vol 25 (4) ◽  
pp. 307-319
Author(s):  
William P. Vignovich ◽  
Vitor H. Pomin
Keyword(s):  
Protein Interactions ◽  
Specific Binding ◽  
Coagulation Factors ◽  
Sulfated Polysaccharides ◽  
Saturation Transfer ◽  
Intermolecular Complexes ◽  
Saturation Transfer Difference ◽  
Protein Partners ◽  
Preferential Binding ◽  
Std Nmr

Novel methods in nuclear magnetic resonance (NMR) spectroscopy have recently been developed to investigate the binding properties of intermolecular complexes endowed with biomedical functions. Among these methods is the saturation transfer difference (STD), which enables the mapping of specific binding motifs of functional ligands. STD can efficiently uncover the specific and preferential binding sites of these ligands in their intermolecular complexes. This is particularly useful in the case of glycosaminoglycans (GAGs), a group of sulfated polysaccharides that play pivotal roles in various biological and pathological processes. The activity of GAGs is ultimately mediated through molecular interactions with key functional proteins, namely, GAG-binding proteins (GBPs). The quality of the GAG-GBP interactions depends on sulfation patterns, oligosaccharide length, and the composing monosaccharides of GAGs. Through STD NMR, information about the atoms of the GAG ligands involved in the complexes is provided. Here we highlight the latest achievements of the literature using STD NMR on GAG oligosaccharide-GBP complexes. Interestingly, most of the GBPs studied so far by STD NMR belong to one of the three major classes: coagulation factors, growth factors, or chemokine/cytokines. Unveiling the structural requirements of GAG ligands in bindings with their protein partners is a crucial step to understand the biochemical and medical actions of GAGs. This process is also a requirement in GAG-based drug discovery and development.

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