[NMR paper] Saturation Transfer Difference NMR and Molecular Docking Interaction Study of Aralkyl-Thiodigalactosides as Potential Inhibitors of the Human-Galectin-3 Protein
Saturation Transfer Difference NMR and Molecular Docking Interaction Study of Aralkyl-Thiodigalactosides as Potential Inhibitors of the Human-Galectin-3 Protein
Human Galectin-3 (hGal-3) is a protein that selectively binds to ?-galactosides and holds diverse roles in both normal and pathological circumstances. Therefore, targeting hGal-3 has become a vibrant area of research in the pharmaceutical chemistry. As a step towards the development of novel hGal-3 inhibitors, we synthesized and investigated derivatives of thiodigalactoside (TDG) modified with different aromatic substituents. Specifically, we describe a high-yielding synthetic route of...
[NMR paper] Identification of new inhibitors of NS5 from dengue virus using saturation transfer difference (STD-NMR) and molecular docking studies
Identification of new inhibitors of NS5 from dengue virus using saturation transfer difference (STD-NMR) and molecular docking studies
The rapid spread of dengue virus has now emerged as a major health problem worldwide, particularly in tropical and sub-tropical regions. Nearly half of the human population is at risk of getting infection. Among the proteomes of dengue virus, nonstructural protein NS5 is conserved across the genus Flavivirus. NS5 comprises methyltransferase enzyme (MTase) domain, which helps in viral RNA capping, and RNA-dependent RNA polymerase (RdRp) domain, which is...
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[NMR paper] Molecular study of mucin-procyanidin interaction by fluorescence quenching and Saturation Transfer Difference (STD)-NMR.
Molecular study of mucin-procyanidin interaction by fluorescence quenching and Saturation Transfer Difference (STD)-NMR.
Related Articles Molecular study of mucin-procyanidin interaction by fluorescence quenching and Saturation Transfer Difference (STD)-NMR.
Food Chem. 2017 Aug 01;228:427-434
Authors: Brandão E, Santos Silva M, García-Estévez I, Mateus N, de Freitas V, Soares S
Abstract
Astringency is closely related to the interaction between procyanidins and salivary proteins (SP). The aim of this work was to study the...
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03-21-2017 11:26 PM
[NMR paper] Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR.
Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR.
FEBS Lett. 2016 Apr;590(7):943-53
Authors: Benoni R, Pertinhez TA, Spyrakis F, Davalli S, Pellegrino S,...
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08-31-2016 02:34 PM
[NMR paper] Molecular Level Insights on Collagen-Polyphenols Interaction using Spin-Relaxation and Saturation Transfer Difference NMR.
Molecular Level Insights on Collagen-Polyphenols Interaction using Spin-Relaxation and Saturation Transfer Difference NMR.
Related Articles Molecular Level Insights on Collagen-Polyphenols Interaction using Spin-Relaxation and Saturation Transfer Difference NMR.
J Phys Chem B. 2015 Oct 8;
Authors: Reddy RR, Phani Kumar BV, Shanmugam G, Madhan B, Mandal AB
Abstract
Interaction of small molecules with collagen has far reaching consequences in biological and industrial processes. The interaction between collagen and selected...
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10-09-2015 04:49 PM
[NMR paper] Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Related Articles Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Anal Bioanal Chem. 2014 Mar 25;
Authors: Yu F, Roy S, Arevalo E, Schaeck J, Wang J, Holte K, Duffner J, Gunay NS, Capila I, Kaundinya GV
Abstract
The binding affinity and specificity of heparin to proteins is widely recognized to be sulfation-pattern dependent. However, for the majority of heparin-binding proteins (HBPs), it still remains...
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03-26-2014 12:44 PM
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
J Biol Inorg Chem. 2011 Apr 3;
Authors: Teixeira JM, Dias DM, Cañada FJ, Martins JA, André JP, Jiménez-Barbero J, Geraldes CF
The study of ligand-receptor interactions using high-resolution NMR techniques, namely the saturation transfer difference (STD),...
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04-05-2011 10:22 PM
[NMR paper] Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Related Articles Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
J Am Chem Soc. 2005 Sep 28;127(38):13110-1
Authors: Soubias O, Gawrisch K
We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR). The results indicate a strong preference for interaction of rhodopsin with the...
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12-01-2010 06:56 PM
[NMR paper] Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experim
Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase.
Related Articles Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase.
Proteins. 2004 Aug 1;56(2):346-53
Authors: Haselhorst T, Wilson JC, Thomson RJ, McAtamney S, Menting JG, Coppel RL, von Itzstein M
Saturation transfer difference...