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Thermal Aggregation of Bovine Serum Albumin in Conventional Buffers: An Insight into Molecular Level Interactions

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Abstract

We have studied the effect of some conventional buffers, which are used frequently for biological research, on the thermal aggregation behavior of bovine serum albumin (BSA). The aggregation kinetics of BSA in buffer solutions were investigated by using UV–Vis spectroscopy. The buffers include sodium phosphate buffer, TRIS buffer and imidazole buffer at physiological pH (7.4). Dynamic light scattering and scanning electron microscopy have been employed to illustrate the size and morphology of protein aggregates. The molecular level interactions of buffer molecules with BSA was probed by various spectroscopic techniques, including UV–Vis, fluorescence, and circular dichroism. The results of this study reveal that the strong interactions of the buffers with protein’s folded/unfolded structures lead to stabilization/destabilization of BSA. We have also explored the possible binding sites of BSA for these buffers using a molecular docking technique.

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Acknowledgements

Ministry MHRD, New Delhi is highly acknowledged for financial support and the authors are acknowledging the Department of Chemistry (NIT Rourkela) for extending their support in terms of the facility to carry out the experiments. Authors are exceptionally thankful to Ms. A. Baral from IMMT, Bhubaneswar for her assistance in carrying out scanning electron microscope (SEM) analysis.

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Authors and Affiliations

  1. Department of Chemistry, National Institute of Technology, Rourkela, Rourkela, Odisha, 769008, India

    Lakkoji Satish, Sabera Millan, Satyabrata Das, Sarita Jena & Harekrushna Sahoo

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  1. Lakkoji Satish
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  2. Sabera Millan
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  3. Satyabrata Das
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  4. Sarita Jena
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  5. Harekrushna Sahoo
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Correspondence to Harekrushna Sahoo.

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Satish, L., Millan, S., Das, S. et al. Thermal Aggregation of Bovine Serum Albumin in Conventional Buffers: An Insight into Molecular Level Interactions. J Solution Chem 46, 831–848 (2017). https://doi.org/10.1007/s10953-017-0612-0

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  • DOI: https://doi.org/10.1007/s10953-017-0612-0

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