Abstract
Protein–protein interaction in solution strongly depends on dissolved ions and solution pH. Interaction among globular protein (bovine serum albumin, BSA), above and below of its isoelectric point (pI ≈ 4.8), is studied in the presence of anions (Cl–, Br–, I–, F–, SO42–) using small-angle neutron scattering (SANS) technique. The SANS study reveals that the short-range attraction among BSA molecules remains nearly unchanged in the presence of anions, whereas the intermediate-range repulsive interaction increases following the Hofmeister series of anions. Although the interaction strength modifies below and above the pI of BSA, it nearly follows the series.
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Acknowledgements
SP acknowledges the Department of Science and Technology, Govt. of India, for the financial support through INSPIRE Fellowship (IF 160402). SK acknowledges financial support from the Department of Science and Technology, Govt. of India. Both the authors acknowledge IASST, Guwahati, for the financial and other experimental facilities.
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SP obtained the financial support through INSPIRE Fellowship (Grant no. IF 160402) supported by the Department of Science and Technology, Govt. of India.
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SP, SK, and VKA performed all the experiments, analysed the data, and wrote the manuscript. SK and VKA validated and supervised the work. All approved the manuscript.
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Pandit, S., Kundu, S. & Aswal, V.K. Interaction among bovine serum albumin (BSA) molecules in the presence of anions: a small-angle neutron scattering study. J Biol Phys 48, 237–251 (2022). https://doi.org/10.1007/s10867-022-09608-w
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DOI: https://doi.org/10.1007/s10867-022-09608-w