Energetic domains and conformational analysis of human serum albumin upon co-incubation with sodium benzoate and glucose

Sodium benzoate (SB), a powerful inhibitor of microbial growth, is one of the most commonly used food preservative. Here, we determined the effects of SB on human serum albumin (HSA) structure in the presence or absence of glucose after 35 days of incubation under physiological conditions. The bioch...

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Published in:Journal of biomolecular structure & dynamics 2014-03, Vol.32 (3), p.438-447
Main Authors: Taghavi, F., Moosavi-Movahedi, A.A., Bohlooli, M., Habibi-Rezaei, M., Hadi Alijanvand, H., Amanlou, M., Sheibani, N., Saboury, A.A., Ahmad, F.
Format: Article
Language:English
Subjects:
DSC
Food Preservatives - chemistry
Glucose - chemistry
human serum albumin
Humans
industrial preservative
Molecular Docking Simulation
prolonged co-incubation
Protein Conformation
Protein Unfolding
Serum Albumin - chemistry
sodium benzoate
Sodium Benzoate - chemistry
thermodynamic analysis
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Summary:Sodium benzoate (SB), a powerful inhibitor of microbial growth, is one of the most commonly used food preservative. Here, we determined the effects of SB on human serum albumin (HSA) structure in the presence or absence of glucose after 35 days of incubation under physiological conditions. The biochemical, biophysical, and molecular approaches including free amine content assay (TNBSA assay), fluorescence, and circular dichroism spectroscopy (CD), differential scanning calorimetry (DSC), and molecular docking and LIGPLOT studies were utilized for structural studies. The TNBSA results indicated that SB has the ability to bind Lys residues in HSA through covalent bonds. The docking and LIGPLOT studies also determined another specific site via hydrophobic interactions. The CD results showed more structural helicity for HSA incubated with SB, while HSA incubated with glucose had the least, and HSA incubated with glucose + SB had medium helicity. Fluorescence spectrophotometry results demonstrated partial unfolding of HSA incubated with SB in the presence or absence of glucose, while maximum partial unfolding was observed in HSA incubated with glucose. These results were confirmed by DSC and its deconvoluted thermograms. The DSC results also showed significant changes in HSA energetic structural domains due to HSA incubation with SB in the presence or absence of glucose. Together, our studies showed the formation of three different intermediates and indicate that biomolecular investigation are effective in providing new insight into safety determinations especially in health-related conditions including diabetes.
ISSN:0739-1102
1538-0254
DOI:10.1080/07391102.2013.775599