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Drug binding to human serum albumin: Abridged review of results obtained with high‐performance liquid chromatography and circular dichroism
Author(s) -
Ascoli Giorgio A.,
Domenici Enrico,
Bertucci Carlo
Publication year - 2006
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.20301
Subject(s) - chemistry , circular dichroism , human serum albumin , drug , plasma protein binding , albumin , pharmacokinetics , serum albumin , blood proteins , pharmacology , chromatography , biochemistry , medicine
The drug binding to plasma and tissue proteins are fundamental factors in determining the overall pharmacological activity of a drug. Human serum albumin (HSA), together with α 1 ‐acid glycoprotein (AGP), are the most important plasma proteins, which act as drug carriers, with drug pharmacokinetic implications, resulting in important clinical impacts for drugs that have a relatively narrow therapeutic index. This review focuses on the combination of biochromatography and circular dichroism as an effective approach for the characterization of albumin binding sites and their enantioselectivity. Furthermore, their applications to the study of changes in the binding properties of the protein arising by the reversible or covalent binding of drugs are discussed, and examples of physiological relevance reported. Perspectives of these studies reside in supporting the development of new drugs, which require miniaturization to facilitate the screening of classes of compounds for their binding to the target protein, and a deeper characterization of the mechanisms involved in the molecular recognition processes. Chirality, 2006. © 2006 Wiley‐Liss, Inc.