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 language | English |
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Pages (from-to) | 270-274 |
Number of pages | 5 |
Journal | ChemPhysChem |
Volume | 12 |
Issue number | 2 |
DOIs | |
Publication status | Published - Feb 7 2011 |
Keywords
- FRET
- drug-binding sites
- fluorescence
- human serum albumin protein
- protein-ligand interactions
ASJC Scopus subject areas
- Atomic and Molecular Physics, and Optics
- Physical and Theoretical Chemistry