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Co-amoxiclav Effects on the Structural and Binding Properties of Human Serum Albumin

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Publisher Brieflands
Specialty Pharmacology
Date 2013 Dec 24
PMID 24363734
Citations 2
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Abstract

Human serum albumin (HSA) is the most abundant plasma protein in the human body. HSA plays an important role in drug transport and metabolism. This protein has a high affinity to a very wide range of materials, including metals such as Cu2+ and Zn2+, fatty acids, amino acids and metabolites such as bilirubin and many drug compounds. In this study, we investigated the effects of co-amoxiclav, as a drug which could be carried by this protein, on HSA structure and binding properties via spectroscopy and electrochemistry techniques. Based on this study, it was found that a therapeutic dose of co-amoxiclav as well as doses 4 to 8 folds higher than the therapeutic dose has no considerable effect on the HSA tertiary structure at 37(o)C. However, a dose 2 folds that of the therapeutic dose has a slight effect, but higher doses of the drug has a mild effect in pathological temperature (42(o)C). In addition, charge density of HSA surface is decreased at 42(o)C, compared to 37(o)C. Hence, this finding suggests a reduced role of HSA in regulation of osmotic pressure in the fever conditions, compared to the physiological conditions. Co-amoxiclav reduces the charge surface density of HSA at physiological and pathological temperatures and therefore alters its binding properties, which could be important in drug interference and complications.

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