Determination of potential scaffolds for human choline kinase α1 by chemical deconvolution studies

María Sahún-Roncero; Belén Rubio-Ruíz; Ana Conejo-García; Adrián Velázquez-Campoy; Antonio Entrena; Ramon Hurtado-Guerrero

doi:10.1002/cbic.201300195

Determination of potential scaffolds for human choline kinase α1 by chemical deconvolution studies

María Sahún-Roncero, Belén Rubio-Ruíz, Ana Conejo-García, Adrián Velázquez-Campoy, Antonio Entrena, Ramon Hurtado-Guerrero

Research output: Contribution to journal › Article › peer-review

Abstract

Dual binding modes: Combined empirical and computational studies of a series of compounds showed adenine and 1-benzyl-4-(dimethylamino)pyridinium fragments to function most efficiently in binding CHOKα1, and also determined how the latter fragment interacts with the choline binding site through two different binding modes. These data provide a basis for the future design of better and more selective inhibitors.

Original language	English
Pages (from-to)	1291-5
Number of pages	5
Journal	ChemBioChem
Volume	14
Issue number	11
DOIs	https://doi.org/10.1002/cbic.201300195
Publication status	Published - 22 Jul 2013

Keywords / Materials (for Non-textual outputs)

Adenine
Binding Sites
Catalytic Domain
Choline Kinase
Humans
Molecular Docking Simulation
Protein Binding
Spectrometry, Fluorescence

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10.1002/cbic.201300195

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title = "Determination of potential scaffolds for human choline kinase α1 by chemical deconvolution studies",

abstract = "Dual binding modes: Combined empirical and computational studies of a series of compounds showed adenine and 1-benzyl-4-(dimethylamino)pyridinium fragments to function most efficiently in binding CHOKα1, and also determined how the latter fragment interacts with the choline binding site through two different binding modes. These data provide a basis for the future design of better and more selective inhibitors.",

keywords = "Adenine, Binding Sites, Catalytic Domain, Choline Kinase, Humans, Molecular Docking Simulation, Protein Binding, Spectrometry, Fluorescence",

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AU - Sahún-Roncero, María

AU - Rubio-Ruíz, Belén

AU - Conejo-García, Ana

AU - Velázquez-Campoy, Adrián

AU - Entrena, Antonio

AU - Hurtado-Guerrero, Ramon

PY - 2013/7/22

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AB - Dual binding modes: Combined empirical and computational studies of a series of compounds showed adenine and 1-benzyl-4-(dimethylamino)pyridinium fragments to function most efficiently in binding CHOKα1, and also determined how the latter fragment interacts with the choline binding site through two different binding modes. These data provide a basis for the future design of better and more selective inhibitors.

KW - Adenine

KW - Binding Sites

KW - Catalytic Domain

KW - Choline Kinase

KW - Humans

KW - Molecular Docking Simulation

KW - Protein Binding

KW - Spectrometry, Fluorescence

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DO - 10.1002/cbic.201300195

M3 - Article

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JO - ChemBioChem

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IS - 11

ER -

Determination of potential scaffolds for human choline kinase α1 by chemical deconvolution studies

Abstract

Keywords / Materials (for Non-textual outputs)

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