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

2010; Wiley; Volume: 12; Issue: 2 Linguagem: Inglês

10.1002/cphc.201000742

1439-7641

Osama K. Abou‐Zied, Najla Al‐Lawatia,

Monoclonal and Polyclonal Antibodies Research

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. Detailed facts of importance to specialist readers are published as "Supporting Information". Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.