Effect of Protein-Protein Interactions on Translational Diffusion of Spheroidal Proteins

One of the commonly accepted approaches to estimate protein-protein interactions (PPI) in aqueous solutions is the analysis of their translational diffusion. The present review article observes a phenomenological approach to analyze PPI effects via concentration dependencies of self- and collective translational diffusion coefficient for several spheroidal proteins derived from the pulsed field gradient NMR (PFG NMR) and dynamic light scattering (DLS), respectively. These proteins are rigid globular alpha-chymotrypsin (ChTr) and human serum albumin (HSA), and partly disordered alpha-casein (alpha-CN) and beta-lactoglobulin (beta-Lg). The PPI analysis enabled us to reveal the dominance of intermolecular repulsion at low ionic strength of solution (0.003-0.01 M) for all studied proteins. The increase in the ionic strength to 0.1-1.0 M leads to the screening of protein charges, resulting in the decrease of the protein electrostatic potential. The increase of the van der Waals potential for ChTr and alpha-CN characterizes their propensity towards unstable weak attractive interactions. The decrease of van der Waals interactions for beta-Lg is probably associated with the formation of stable oligomers by this protein. The PPI, estimated with the help of interaction potential and idealized spherical molecular geometry, are in good agreement with experimental data.

Automated summary

This review article analyzes the effects of protein-protein interactions (PPI) using a phenomenological approach. The study reveals the dominance of intermolecular repulsion at low ionic strength and the screening of protein charges at higher ionic strength. The change in van der Waals potential also reflects the propensity of different proteins towards specific types of interactions.