scholarly journals Correction to “Examining Binding to Nanoparticle Surfaces Using Saturation Transfer Difference (STD)-NMR Spectroscopy”

2019 ◽  
Vol 124 (1) ◽  
pp. 1249-1249
Author(s):  
Yunzhi Zhang ◽  
Hui Xu ◽  
Austin M. Parsons ◽  
Leah B. Casabianca
Keyword(s):  
Nmr Spectroscopy ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Std Nmr

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

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.

scholarly journals Spin ballet for sweet encounters: saturation-transfer difference NMR and X-ray crystallography complement each other in the elucidation of protein–glycan interactions

2018 ◽  
Vol 74 (8) ◽  
pp. 451-462 ◽  
Author(s):  
Bärbel S. Blaum ◽  
Ursula Neu ◽  
Thomas Peters ◽  
Thilo Stehle
Keyword(s):  
Nmr Spectroscopy ◽  
Structural Biology ◽  
Protein Structures ◽  
Saturation Transfer ◽  
Ligand Complex ◽  
Isotope Labelling ◽  
Size Limit ◽  
Protein Size ◽  
Saturation Transfer Difference ◽  
Std Nmr

Biomolecular NMR spectroscopy has limitations in the determination of protein structures: an inherent size limit and the requirement for expensive and potentially difficult isotope labelling pose considerable hurdles. Therefore, structural analysis of larger proteins is almost exclusively performed by crystallography. However, the diversity of biological NMR applications outperforms that of any other structural biology technique. For the characterization of transient complexes formed by proteins and small ligands, notably oligosaccharides, one NMR technique has recently proven to be particularly powerful: saturation-transfer difference NMR (STD-NMR) spectroscopy. STD-NMR experiments are fast and simple to set up, with no general protein size limit and no requirement for isotope labelling. The method performs best in the moderate-to-low affinity range that is of interest in most of glycobiology. With small amounts of unlabelled protein, STD-NMR experiments can identify hits from mixtures of potential ligands, characterize mutant proteins and pinpoint binding epitopes on the ligand side. STD-NMR can thus be employed to complement and improve protein–ligand complex models obtained by other structural biology techniques or by purely computational means. With a set of protein–glycan interactions from our own work, this review provides an introduction to the technique for structural biologists. It exemplifies how crystallography and STD-NMR can be combined to elucidate protein–glycan (and other protein–ligand) interactions in atomic detail, and how the technique can extend structural biology from simplified systems amenable to crystallization to more complex biological entities such as membranes, live viruses or entire cells.

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>

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