Glucose and fluoxetine induce fine structural change in human serum albumin

Human serum albumin has been used as a model protein for protein folding and ligand binding studies over many decades. Due to its long life period and high concentration in plasma, HSA is highly sensitive to glycation. It is reported that 175 mg/dL glucose concentration is a threshold of kidney acti...

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Published inIranian journal of pharmaceutical research : IJPR Vol. 12; no. 1; pp. 185 - 191
Main Authors Shahani, Minoo, Daneshi-Mehr, Fatemeh, Tadayon, Roya, Hoseinzade Salavati, Behrooz, Akbar Zadeh-Baghban, Ali-Reza, Zamanian, Abbas, Rezaei-Tavirani, Mostafa
Format Journal Article
LanguageEnglish
Published Iran Shaheed Beheshti University of Medical Sciences 2013
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Summary:Human serum albumin has been used as a model protein for protein folding and ligand binding studies over many decades. Due to its long life period and high concentration in plasma, HSA is highly sensitive to glycation. It is reported that 175 mg/dL glucose concentration is a threshold of kidney activity for the beginning of excretion of glucose. pH denaturation of HSA in absence and presence of different concentrations of glucose is studied and based on the Pace two-state model, the findings are analyzed. In addition, florescence emission data of albumin range in the period of 300-500 nm was depicted. The amounts of free energy change and [D]1/2 parameters of unfolding in correspond to florescence date indicate that glucose induces fine structural change in human serum albumin. Results showed that 175 mg/dL glucose concentration is a critical point for albumin structural and functional alteration.
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ISSN:1735-0328
1726-6890