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Buffer-specific effects arise from ionic dispersion forces
Journal article   Peer reviewed

Buffer-specific effects arise from ionic dispersion forces

D.F. Parsons, C. Carucci and Andrea Salis
Physical Chemistry Chemical Physics, Vol.24(11), pp.6544-6551
2022
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Abstract

Buffer solutions do not simply regulate pH, but also change the properties of protein molecules. The zeta potential of lysozyme varies significantly at the same buffer concentration, in the order Tris > phosphate > citrate, with citrate even inverting the zeta potential, usually positive at pH 7.15, to a negative value. This buffer-specific effect is a special case of the Hofmeister effect. Here we present a theoretical model of these buffer-specific effects using a Poisson–Boltzmann description of the buffer solution, modified to include dispersion forces of all ions interacting with the lysozyme surface. Dispersion coefficients are determined from quantum chemical polarizabilites calculated for each ion for tris, phosphate, and citrate buffer solutions. The lysozyme surface charge is controlled by charge regulation of carboxylate and amine sites of the component amino acids. The theoretical model satisfactorily reproduces experimental zeta potentials, including change of sign with citrate, when hydration of small cosmotropic ions (Na+, H+, OH−) is included.

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Collaboration types
Domestic collaboration
International collaboration
Citation topics
2 Chemistry
2.89 Ionic, Molecular & Complex Liquids
2.89.677 Liquid Water
Web Of Science research areas
Chemistry, Physical
Physics, Atomic, Molecular & Chemical
ESI research areas
Chemistry
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