Journal
MEDICINAL RESEARCH REVIEWS
Volume 23, Issue 3, Pages 275-301Publisher
JOHN WILEY & SONS INC
DOI: 10.1002/med.10039
Keywords
human serum albumin; QSAR; cheminformatics; ADME prediction
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Drug binding to Human Serum Albumin (HSA) is an area of intense research. The pharmacokinetics and pharmacodynamics of drugs are strongly affected by their binding to this protein. In this article, the field is reviewed, as well as our models to predict drug-binding affinities to HSA from drug structure. The physiological role of HSA is described, as well as its influence in drug action. The crystal structures of this protein are discussed, emphasizing the two drug-binding sites and the fatty acids binding sites observed therein. The advantages of using high-performance affinity chromatography to rapidly screen drugs for HSA binding are explained. The different QSAR models for HSA binding of restricted families of drugs (both from other groups and our group) are enumerated. Finally, a detailed description of our general models to predict drug-binding strengths to HSA from structure is given. It is expected for these models to be useful in drug design and pharmaceutical research. (C) 2003 Wiley Periodicals, Inc. Med Res Rev, 23, No. 3, 275-301, 2003.
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