Ligand-Receptor Binding Affinities from Saturation Transfer Difference (STD) NMR Spectroscopy: The Binding Isotherm of STD Initial Growth Rates

2010 ◽  
Vol 16 (26) ◽  
pp. 7803-7812 ◽  
Author(s):  
Jesús Angulo ◽  
Pedro M. Enríquez-Navas ◽  
Pedro M. Nieto
Keyword(s):  
Nmr Spectroscopy ◽  
Receptor Binding ◽  
Growth Rates ◽  
Initial Growth ◽  
Binding Affinities ◽  
Saturation Transfer ◽  
Binding Isotherm ◽  
Saturation Transfer Difference ◽  
Std Nmr

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.

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

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.

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 Saturation Transfer Difference NMR Spectroscopy Using Glycopolymers

2020 ◽  
Author(s):  
janet muzulu ◽  
Amit Basu
Keyword(s):  
Nmr Spectroscopy ◽  
Boronic Acid ◽  
Spin Diffusion ◽  
Amplification Factor ◽  
Boronic Acids ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Experimental Parameters ◽  
Std Nmr ◽  
Phenylboronic Acids

<p>We report the use of Saturation Transfer Difference (STD) NMR spectroscopy to observe the interaction of various phenylboronic acids (PBAs) with synthetic glycopolymers presenting galactose and glucose. After optimizing experimental parameters to maximize spin diffusion, the binding of boronic acids to the glycopolymers was examined using STD NMR. Efficient amplification factor build-up curves which were used to generate an epitope map for the boronic acid binding to the glycopolymers. STD-NMR was also used to detect the interaction between indole and a galactosylated glycopolymer, providing an indole-based view of this C-H – π interaction.</p>

scholarly journals A COVID Moonshot: assessment of ligand binding to the SARS-CoV-2 main protease by saturation transfer difference NMR spectroscopy

2020 ◽  
Author(s):  
Anastassia L. Kantsadi ◽  
Emma Cattermole ◽  
Minos-Timotheos Matsoukas ◽  
Georgios A. Spyroulias ◽  
Ioannis Vakonakis
Keyword(s):  
Nmr Spectroscopy ◽  
Open Science ◽  
Saturation Transfer ◽  
Ligand Affinity ◽  
Fragment Screening ◽  
Saturation Transfer Difference ◽  
Nmr Data ◽  
Main Protease ◽  
Promising Therapeutic Target ◽  
Std Nmr

AbstractSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the etiological cause of the coronavirus disease 2019, for which no effective therapeutics are available. The SARS-CoV-2 main protease (Mpro) is essential for viral replication and constitutes a promising therapeutic target. Many efforts aimed at deriving effective Mpro inhibitors are currently underway, including an international open-science discovery project, codenamed COVID Moonshot. As part of COVID Moonshot, we used saturation transfer difference nuclear magnetic resonance (STD-NMR) spectroscopy to assess the binding of putative Mpro ligands to the viral protease, including molecules identified by crystallographic fragment screening and novel compounds designed as Mpro inhibitors. In this manner, we aimed to complement enzymatic activity assays of Mpro performed by other groups with information on ligand affinity. We have made the Mpro STD-NMR data publicly available. Here, we provide detailed information on the NMR protocols used and challenges faced, thereby placing these data into context. Our goal is to assist the interpretation of Mpro STD-NMR data, thereby accelerating ongoing drug design efforts.

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