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 journalArticlepeer-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 languageEnglish
Pages (from-to)1291-5
Number of pages5
JournalChemBioChem
Volume14
Issue number11
DOIs
Publication statusPublished - 22 Jul 2013

Keywords

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

Fingerprint

Dive into the research topics of 'Determination of potential scaffolds for human choline kinase α1 by chemical deconvolution studies'. Together they form a unique fingerprint.

Cite this