Int. J. Mol. Sci. 2014, 15(3), 3580-3595; doi:10.3390/ijms15033580

Interactive Association of Drugs Binding to Human Serum Albumin

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Received: 27 January 2014; in revised form: 17 February 2014 / Accepted: 18 February 2014 / Published: 27 February 2014
(This article belongs to the collection Proteins and Protein-Ligand Interactions)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.
Keywords: human serum albumin; binding site; interactions of protein–ligands; interactive associations of drugs; structure of protein complex
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MDPI and ACS Style

Yang, F.; Zhang, Y.; Liang, H. Interactive Association of Drugs Binding to Human Serum Albumin. Int. J. Mol. Sci. 2014, 15, 3580-3595.

AMA Style

Yang F, Zhang Y, Liang H. Interactive Association of Drugs Binding to Human Serum Albumin. International Journal of Molecular Sciences. 2014; 15(3):3580-3595.

Chicago/Turabian Style

Yang, Feng; Zhang, Yao; Liang, Hong. 2014. "Interactive Association of Drugs Binding to Human Serum Albumin." Int. J. Mol. Sci. 15, no. 3: 3580-3595.

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