Related ArticlesOn-cell saturation transfer difference NMR study of Bombesin binding to GRP receptor.
Bioorg Chem. 2020 Apr 18;99:103861
Authors: Palmioli A, Ceresa C, Tripodi F, La Ferla B, Nicolini G, Airoldi C
Abstract
We report the NMR characterization of the molecular interaction between Gastrin Releasing Peptide Receptor (GRP-R) and its natural ligand bombesin (BN). GRP-R is a transmembrane G-protein coupled receptor promoting the stimulation of cancer cell proliferation; in addition, being overexpressed on the surface of different human cancer cell lines, it is ideal for the development of new strategies for the selective targeted delivery of anticancer drugs and diagnostic devices to tumor cells. However, the design of new GRP-R binders requires structural information on receptor interaction with its natural ligands. The experimental protocol presented herein, based on on-cell STD NMR techniques, is a powerful tool for the screening and the epitope mapping of GRP-R ligands aimed at the development of new anticancer and diagnostic tools. Notably, the study can be carried out in a physiological environment, at the surface of tumoral cells overespressing GRP-R. Moreover, to the best of our knowledge, this is the first example of an NMR experiment able to detect and investigate the structural determinants of BN/GRP-R interaction.
PMID: 32339813 [PubMed - as supplied by publisher]
[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] 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] 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
Comparison of the sensitivities of WaterLOGSY and saturation transfer difference NMR experiments
Comparison of the sensitivities of WaterLOGSY and saturation transfer difference NMR experiments
Abstract
The WaterLOGSY (WL) and saturation transfer difference (STD) NMR experiments have proven to be extremely useful techniques to characterize interactions between small molecules and large biomolecules. In this work we compare the relative sensitivities of WL and STD NMR using 3 experimental systems: ketoprofen (KET)â??bovine serum albumin (BSA), tert-butyl hydroquinone (TBHQ)â??hemagglutinin (HA), and chloramphenicol (CAM)â??ribosome (70S). In all...
[NMR paper] Saturation transfer difference NMR for fragment screening.
Saturation transfer difference NMR for fragment screening.
Related Articles Saturation transfer difference NMR for fragment screening.
Curr Protoc Chem Biol. 2013 Dec 1;5(4):251-68
Authors: Begley DW, Moen SO, Pierce PG, Zartler ER
Abstract
Fragment screening by saturation transfer difference nuclear magnetic resonance (STD-NMR) is a robust method for identifying small molecule binders and is well suited to a broad set of biological targets. STD-NMR is exquisitely sensitive for detecting weakly binding compounds (a common characteristic of...
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01-07-2014 11:16 PM
[Question from NMRWiki Q&A forum] Saturation transfer difference TROSY
Saturation transfer difference TROSY
Has anyone added a pulse scheme for cross saturation to their TROSY for Bruker platform?
Could you share a pulse sequence if you have one?
Thanks!
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05-18-2013 09:22 AM
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),...
On-cell saturation transfer difference NMR study of Bombesin binding to GRP receptor.
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