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. 2020 Aug 20;11(16):6805-6811.
doi: 10.1021/acs.jpclett.0c01900. Epub 2020 Aug 7.

Specific Buffer Effects on the Intermolecular Interactions among Protein Molecules at Physiological pH

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Specific Buffer Effects on the Intermolecular Interactions among Protein Molecules at Physiological pH

Andrea Salis et al. J Phys Chem Lett. .

Abstract

BSA and lysozyme molecular motion at pH 7.15 is buffer-specific. Adsorption of buffer ions on protein surfaces modulates the protein surface charge and thus protein-protein interactions. Interactions were estimated by means of the interaction parameter kD obtained from plots of diffusion coefficients at different protein concentrations (Dapp = D0[1 + kDCprotein]) via dynamic light scattering and nuclear magnetic resonance. The obtained results agree with recent findings confirming doubts regarding the validity of the Henderson-Hasselbalch equation, which has traditionally provided a basis for understanding pH buffers of primary importance in solution chemistry, electrochemistry, and biochemistry.

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