Characterization of caged compounds binding to proteins by NMR spectroscopy

Bandorowicz‐Pikuła, Joanna; Buchet, René; Cañada, F. Javier; Clémancey, Martin; Groves, Patrick; Jiménez‐Barbero, Jesús; Lancelin, Jean‐Marc; Marcillat, Olivier; Pikula, Sławomir; Sekrecka-Belniak, Anna; Strzelecka‐Kiliszek, Agnieszka

doi:10.1016/j.bbrc.2010.08.104

Cited by 3 publications

(1 citation statement)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…STD-NMR spectroscopy was used to investigate the binding properties of the caged nucleotides guanosine 5'-O-(3-thiotriphosphate), P 3(S)-(1-(4,5-dimethoxy-2-nitrophenyl)ethyl) ester (DMNPE-GTP-γ-S) and adenosine 5'-diphosphate, P 2 -(1-(2-nitrophenyl)ethyl) ester (NPE-ADP) to rabbit muscle creatine kinase (RMCK) and human annexin A6 (hAnxA6) [56]. The obtained results indicated the strong binding of caged nucleotides to the investigated proteins.…”

Section: Ligand-protein Interactionsmentioning

confidence: 99%

NMR Spectroscopy for Studying Interactions of Bioactive Molecules

Novak¹,

Jednačak²

2012

Physico-Chemical Methods in Drug Discovery and Development

View full text Add to dashboard Cite

Section: Ligand-protein Interactionsmentioning

confidence: 99%

NMR Spectroscopy for Studying Interactions of Bioactive Molecules

Novak¹,

Jednačak²

2012

Physico-Chemical Methods in Drug Discovery and Development

View full text Add to dashboard Cite

Carbohydrate–Protein Interactions: A 3D View by NMR

2011

Self Cite

View full text Add to dashboard Cite

This review focuses on the application of NMR methods for understanding, at the molecular and atomic levels, the diverse mechanisms by which sugar molecules are recognised by the binding sites of lectins, antibodies and enzymes. Given the intrinsic chemical natures of sugars and their flexibility, it is well established that NMR parameters should be complemented by computational methods in attempts to unravel the structural and conformational features of the molecular recognition process unambiguously. We therefore aim here to describe new and significant advances in the knowledge of carbohydrate-protein interactions, obtained by employing state-of-the-art NMR and molecular modelling. We have not attempted to prepare an exhaustive review but have tried to focus on describing the key aspects that should be considered when tackling a problem within this research topic.

show abstract

Exploring NMR methods as a tool to select suitable fluorescent nucleotide analogues

et al. 2013

View full text Add to dashboard Cite

Fluorescent analogues provide important tools for biochemical/biophysical research. However, the analogues contain chemical modifications much larger than those known to affect ligand-binding, such as the inversion of a carbon centre or substitution of an atom. We lack experimental tools and protocols to select the most appropriate fluorescent analogue. Herein, we use several NMR spectroscopy methods, including Saturation Transfer Difference (STD), STD competition and transferred nuclear Overhauser effect spectroscopy (Tr-NOESY), as tools to select appropriate fluorescent probes. Annexin A6 (AnxA6) is a ubiquitous protein that forms in vitro GTP-induced ion channels. We used this protein as a model and screened guanosine triphosphate (GTP) and four fluorescent analogues against AnxA6. STD reported that the GTP moiety of all ligands made similar contacts with the protein, despite additional interactions between the fluorescent tags and AnxA6. Competition STD experiments verified that the analogues and GTP bind to the same site. Tr-NOESY indicated that the bound conformation of the base relative to ribose is altered for some analogues compared to GTP. MANT-GTP or the BODIPY thioester of guanosine 5'-O-(3-thiotriphosphate) are the most suitable fluorescent analogues for AnxA6, according to NMR. These results reveal NMR as a useful technique to select and design proper fluorescent tags for biochemical/biophysical assays.

show abstract

Characterization of caged compounds binding to proteins by NMR spectroscopy

Abstract: El artículo seleccionado no se encuentra disponible por ahora a texto completo por no haber sido facilitado todavía por el investigador a cargo del archivo del mismo.

Cited by 3 publications

References 43 publications

NMR Spectroscopy for Studying Interactions of Bioactive Molecules

NMR Spectroscopy for Studying Interactions of Bioactive Molecules

Carbohydrate–Protein Interactions: A 3D View by NMR

Exploring NMR methods as a tool to select suitable fluorescent nucleotide analogues

Contact Info

Product

Resources

About