Co-amoxiclav Effects on the Structural and Binding Properties of Human Serum Albumin
| Author | Saeed Hesami Takallu | en |
| Author | Mostafa Rezaei Tavirani | en |
| Author | Shiva Kalantari | en |
| Author | Mahrooz Amir Bakhtiarvand | en |
| Author | Sayed Mohammad Mahdavi | en |
| Issued Date | 2010-07-31 | en |
| 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 37oC. 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 (42oC). In addition, charge density of HSA surface is decreased at 42oC, compared to 37oC. 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. | en |
| DOI | https://doi.org/10.22037/ijpr.2010.863 | en |
| Keyword | Human serum albumin | en |
| Keyword | Co-amoxiclav | en |
| Keyword | Charge surface density | en |
| Keyword | Fever | en |
| Keyword | Hexadecyl pyridinium bromide | en |
| Publisher | Brieflands | en |
| Title | Co-amoxiclav Effects on the Structural and Binding Properties of Human Serum Albumin | en |
| Type | Original Article | en |
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