We have combined saturation transfer difference NMR (STD NMR) with chemical shift imaging (CSI) and controlled concentration gradients of small molecule ligands to develop imaging STD NMR, a new tool for the assessment of protein-ligand interactions. Our methodology allows the determination of protein-ligand dissociation constants (K(D)) and assessment of the binding specificity in a single NMR tube, avoiding time-consuming titrations. We demonstrate the formation of suitable and reproducible...
[NMR paper] Detecting and Characterizing Interactions of Metabolites with Proteins by Saturation Transfer Difference Nuclear Magnetic Resonance (STD NMR) Spectroscopy
Detecting and Characterizing Interactions of Metabolites with Proteins by Saturation Transfer Difference Nuclear Magnetic Resonance (STD NMR) Spectroscopy
Saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopy is an established technique for detecting and characterizing the binding of small molecules, such as metabolites, to biological macromolecules like proteins and nucleic acids. STD NMR allows detection of binding in complex mixtures of potential ligands, which is often used for library screening in the pharmaceutical industry but may also be beneficial for...
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A COVID moonshot: assessment of ligand binding to the SARS-CoV-2 main protease by saturation transfer difference NMR spectroscopy
A COVID moonshot: assessment of ligand binding to the SARS-CoV-2 main protease by saturation transfer difference NMR spectroscopy
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the etiological cause of the coronavirus disease 2019, for which no effective antiviral 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...
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04-15-2021 12:12 PM
[NMR paper] Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy.
Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy.
Related Articles Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy.
Angew Chem Int Ed Engl. 1999 Jun 14;38(12):1784-1788
Authors: Mayer M, Meyer B
Abstract
Fast identification of binding activity directly from mixtures of potential ligands is possible with the NMR method described, which is based on saturation transfer to molecules in direct contact to a protein. In addition, the ligand's binding epitope is...
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05-03-2018 06:46 PM
[NMR paper] Determinants of ligand subtype-selectivity at ?1A-adrenoceptor revealed using Saturation Transfer Difference (STD) NMR.
Determinants of ligand subtype-selectivity at ?1A-adrenoceptor revealed using Saturation Transfer Difference (STD) NMR.
Determinants of ligand subtype-selectivity at ?1A-adrenoceptor revealed using Saturation Transfer Difference (STD) NMR.
ACS Chem Biol. 2018 Mar 14;:
Authors: Yong KJ, Vaid TM, Shilling PJ, Wu FJ, Williams LM, Deluigi M, Plückthun A, Bathgate RA, Gooley PR, Scott DJ
Abstract
?1A- and ?1B-adrenoceptors (?1A-AR and ?1B-AR) are closely related G protein-coupled receptors (GPCRs) that modulate the cardiovascular and...
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03-15-2018 02:29 PM
[NMR paper] The Quest for Anticancer Vaccines: Deciphering the Fine-Epitope Specificity of Cancer-Related Monoclonal Antibodies by Combining Microarray Screening and Saturation Transfer Difference NMR.
The Quest for Anticancer Vaccines: Deciphering the Fine-Epitope Specificity of Cancer-Related Monoclonal Antibodies by Combining Microarray Screening and Saturation Transfer Difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles The Quest for Anticancer Vaccines: Deciphering the Fine-Epitope Specificity of Cancer-Related Monoclonal Antibodies by Combining Microarray Screening and Saturation Transfer Difference NMR.
J Am Chem Soc. 2015 Oct 7;137(39):12438-41
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04-21-2016 06:37 PM
[NMR paper] Structural Analysis of CXCR4 - Antagonist Interactions Using Saturation-Transfer Double-Difference NMR.
Structural Analysis of CXCR4 - Antagonist Interactions Using Saturation-Transfer Double-Difference NMR.
Related Articles Structural Analysis of CXCR4 - Antagonist Interactions Using Saturation-Transfer Double-Difference NMR.
Biochem Biophys Res Commun. 2015 Aug 21;
Authors: Cox BD, Mehta AK, DiRaddo JO, Liotta DC, Wilson LJ, Snyder JP
Abstract
CXCR4 is a GPCR involved in leukocyte trafficking. Small molecule antagonists of the receptor may treat inflammatory disease, cancer and HIV. Here we probe the binding of a...
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08-25-2015 08:30 PM
[NMR paper] Specific RNA-protein interactions detected with saturation transfer difference NMR.
Specific RNA-protein interactions detected with saturation transfer difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.landesbioscience.com-icon-pubmed-Landesbioscience2.jpg Specific RNA-protein interactions detected with saturation transfer difference NMR.
RNA Biol. 2013 Jul 30;10(8)
Authors: Harris KA, Shekhtman A, Agris PF
Abstract
RNA, at the forefront of biochemical research due to its central role in biology, is recognized by proteins through various mechanisms. Analysis of the...
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08-21-2013 08:49 PM
[NMR paper] Monomer-collagen interactions studied by saturation transfer difference NMR.
Monomer-collagen interactions studied by saturation transfer difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-sage.gif Related Articles Monomer-collagen interactions studied by saturation transfer difference NMR.
J Dent Res. 2013 Mar;92(3):284-8
Authors: Hiraishi N, Tochio N, Kigawa T, Otsuki M, Tagami J
Abstract
Functional monomers in dentin adhesives are involved in wetting dental substrates, demineralization, and the formation of calcium salts....
Imaging Saturation Transfer Difference (STD) NMR: Affinity and Specificity of Protein-Ligand Interactions from a Single NMR Sample
Linear Mode
