A Murine Monoclonal Antibody to Glycogen: Characterization of Epitope-Fine Specificity by Saturation Transfer Difference (STD) NMR Spectroscopy and Its Use in Mycobacterial Capsular α-Glucan Research

ChemBioChem ◽  
2015 ◽  
Vol 16 (6) ◽  
pp. 977-989 ◽  
Author(s):  
Robert van de Weerd ◽  
M. Alvaro Berbís ◽  
Marrion Sparrius ◽  
Janneke J. Maaskant ◽  
Maikel Boot ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Nmr Spectroscopy ◽  
Murine Monoclonal Antibody ◽  
Saturation Transfer ◽  
Fine Specificity ◽  
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

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 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 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
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