[NMR paper] Insights on the Interaction between Transthyretin and A? in Solution. A Saturation Transfer Difference (STD) NMR Analysis of the Role of Iododiflunisal.
Insights on the Interaction between Transthyretin and A? in Solution. A Saturation Transfer Difference (STD) NMR Analysis of the Role of Iododiflunisal.
Related ArticlesInsights on the Interaction between Transthyretin and A? in Solution. A Saturation Transfer Difference (STD) NMR Analysis of the Role of Iododiflunisal.
J Med Chem. 2017 Jul 13;60(13):5749-5758
Authors: Gimeno A, Santos LM, Alemi M, Rivas J, Blasi D, Cotrina EY, Llop J, Valencia G, Cardoso I, Quintana J, Arsequell G, Jiménez-Barbero J
Abstract
Several strategies against Alzheimer disease (AD) are directed to target A?-peptides. The ability of transthyretin (TTR) to bind A?-peptides and the positive effect exerted by some TTR stabilizers for modulating the TTR-A? interaction have been previously studied. Herein, key structural features of the interaction between TTR and the A?(12-28) peptide (3), the essential recognition element of A?, have been unravelled by STD-NMR spectroscopy methods in solution. Molecular aspects related to the role of the TTR stabilizer iododiflunisal (IDIF, 5) on the TTR-A? complex have been also examined. The NMR results, assisted by molecular modeling protocols, have provided a structural model for the TTR-A? interaction, as well as for the ternary complex formed in the presence of IDIF. This basic structural information could be relevant for providing light on the mechanisms involved in the ameliorating effects of AD symptoms observed in AD/TTR(±) animal models after IDIF treatment and eventually for designing new molecules toward AD therapeutic drugs.
[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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[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] NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
Methods Mol Biol. 2014;1200:501-9
Authors: Hemmi H
Abstract
One of the most commonly used...
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04-09-2015 03:47 AM
[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
[NMR paper] Role of 2-Hydroxyethyl Methacrylate in the Interaction of Dental Monomers with Collagen Studied by Saturation Transfer Difference NMR.
Role of 2-Hydroxyethyl Methacrylate in the Interaction of Dental Monomers with Collagen Studied by Saturation Transfer Difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Role of 2-Hydroxyethyl Methacrylate in the Interaction of Dental Monomers with Collagen Studied by Saturation Transfer Difference NMR.
J Dent. 2014 Jan 16;
Authors: Hiraishi N, Tochio N, Kigawa T, Otsuki M, Tagam J
Abstract
Objections: Functional adhesive monomers...
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01-21-2014 11:10 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...