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

Andrea Salis, Luca Cappai, Cristina Carucci, Drew F. Parsons, Maura Monduzzi

The Journal of Physical Chemistry Letters · 2020 · 54 citations · 52 references

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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 <i>k</i><sub>D</sub> obtained from plots of diffusion coefficients at different protein concentrations (<i>D</i><sub>app</sub> = <i>D</i><sub>0</sub>[1 + <i>k</i><sub>D</sub><i>C</i><sub>protein</sub>]) 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.

References

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