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Int J Mol Sci. 2014 Feb 27;15(3):3580-95. doi: 10.3390/ijms15033580.

Interactive association of drugs binding to human serum albumin.

International journal of molecular sciences

Feng Yang, Yao Zhang, Hong Liang

Affiliations

  1. State Key Laboratory Cultivation Base for the Chemistry and Molecular Engineering of Medicinal Resources, Ministry of Science and Technology of China, Guangxi Normal University, Guilin 541000, Guangxi, China. [email protected].
  2. State Key Laboratory Cultivation Base for the Chemistry and Molecular Engineering of Medicinal Resources, Ministry of Science and Technology of China, Guangxi Normal University, Guilin 541000, Guangxi, China. [email protected].
  3. State Key Laboratory Cultivation Base for the Chemistry and Molecular Engineering of Medicinal Resources, Ministry of Science and Technology of China, Guangxi Normal University, Guilin 541000, Guangxi, China. [email protected].

PMID: 24583848 PMCID: PMC3975355 DOI: 10.3390/ijms15033580

Abstract

Human serum albumin (HSA) is an abundant plasma protein, which attracts great interest in the pharmaceutical industry since it can bind a remarkable variety of drugs impacting their delivery and efficacy and ultimately altering the drug's pharmacokinetic and pharmacodynamic properties. Additionally, HSA is widely used in clinical settings as a drug delivery system due to its potential for improving targeting while decreasing the side effects of drugs. It is thus of great importance from the viewpoint of pharmaceutical sciences to clarify the structure, function, and properties of HSA-drug complexes. This review will succinctly outline the properties of binding site of drugs in IIA subdomain within the structure of HSA. We will also give an overview on the binding characterization of interactive association of drugs to human serum albumin that may potentially lead to significant clinical applications.

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