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

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

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.

MeSH terms

  • Animals
  • Buffers
  • Cattle
  • Chickens
  • Citric Acid / chemistry
  • Hydrogen-Ion Concentration
  • Muramidase / chemistry
  • Muramidase / metabolism*
  • Phosphates / chemistry
  • Protein Binding
  • Protein Multimerization
  • Serum Albumin, Bovine / chemistry
  • Serum Albumin, Bovine / metabolism*
  • Static Electricity
  • Tromethamine / chemistry

Substances

  • Buffers
  • Phosphates
  • Tromethamine
  • Serum Albumin, Bovine
  • Citric Acid
  • hen egg lysozyme
  • Muramidase