scholarly journals Unveiling the “Three-Finger Pharmacophore” Required for p53-MDM2 Inhibition by Saturation-Transfer Difference (STD) NMR Initial Growth-Rates Approach

2016 ◽  
Vol 22 (17) ◽  
pp. 5858-5862 ◽  
Author(s):  
Jesus Angulo ◽  
Sarah A. Goffin ◽  
Daivik Gandhi ◽  
Mark Searcey ◽  
Lesley A. Howell
Keyword(s):  
Growth Rates ◽  
Initial Growth ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Std Nmr

scholarly journals Kinetics of intramolecular chemical exchange by initial growth rates of spin saturation transfer difference experiments (SSTD NMR)

2015 ◽  
Vol 51 (50) ◽  
pp. 10222-10225 ◽  
Author(s):  
M. Teresa Quirós ◽  
Jesús Angulo ◽  
María Paz Muñoz
Keyword(s):  
Kinetic Parameters ◽  
Growth Rates ◽  
Chemical Exchange ◽  
Initial Growth ◽  
Saturation Transfer ◽  
Nmr Method ◽  
Saturation Transfer Difference ◽  
Kinetics Of

Initial growth rates SSTD NMR method is a new powerful tool to obtain the kinetic parameters of intramolecular chemical exchange.

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.

Examining Binding to Nanoparticle Surfaces Using Saturation Transfer Difference (STD)-NMR Spectroscopy

2017 ◽  
Vol 121 (44) ◽  
pp. 24678-24686 ◽  
Author(s):  
Yunzhi Zhang ◽  
Hui Xu ◽  
Austin M. Parsons ◽  
Leah B. Casabianca
Keyword(s):  
Nmr Spectroscopy ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Std Nmr

Molecular study of mucin-procyanidin interaction by fluorescence quenching and Saturation Transfer Difference (STD)-NMR

2017 ◽  
Vol 228 ◽  
pp. 427-434 ◽  
Author(s):  
Elsa Brandão ◽  
Mafalda Santos Silva ◽  
Ignacio García-Estévez ◽  
Nuno Mateus ◽  
Victor de Freitas ◽  
...  
Keyword(s):  
Fluorescence Quenching ◽  
Molecular Study ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Std Nmr

scholarly journals Characterizing the interaction between methyl ferulate and human serum albumin by saturation transfer difference NMR

RSC Advances ◽  
2020 ◽  
Vol 10 (54) ◽  
pp. 32999-33009
Author(s):  
Wenjing Wang ◽  
Qiaomei Sun ◽  
Na Gan ◽  
Yuanming Zhai ◽  
Hongzhao Xiang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Saturation Transfer ◽  
Recognition Mechanism ◽  
Saturation Transfer Difference ◽  
Std Nmr ◽  
Methyl Ferulate

STD-NMR technique characterized the recognition mechanism of methyl ferulate and human serum albumin qualitatively and quantitatively.

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