Exploring the Drug-Binding Site Sudlow i of Human Serum Albumin: The Role of Water and Trp214 in Molecular Recognition and Ligand Binding

Osama K. Abou-Zied, Najla Al-Lawatia

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

Choosy: Three hydroxyquinolines (HQs) are used as probes to reveal more details about the binding nature of one of the major drug-binding sites of human serum albumin (Sudlow I) and to unravel the local environment around the probes in the binding site. The results (see picture) indicate the existence of water in the binding site and that a selective interaction between HQs and Trp214 in the native state unmasks the tyrosine fluorescence.

Original languageEnglish
Pages (from-to)270-274
Number of pages5
JournalChemPhysChem
Volume12
Issue number2
DOIs
Publication statusPublished - Feb 7 2011

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Keywords

  • drug-binding sites
  • fluorescence
  • FRET
  • human serum albumin protein
  • protein-ligand interactions

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Atomic and Molecular Physics, and Optics

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