Combined Effects of Pressure and Ionic Strength on Protein–Protein Interactions: An Empirical Approach
Date
2024-01-08
Journal Title
Journal ISSN
Volume Title
Publisher
Biomacromolecules
Abstract
Proteins are exposed to hydrostatic pressure (HP) in a variety of ecosystems as well as in processing steps such as freeze–thaw, cell disruption, sterilization, and homogenization, yet pressure effects on protein–protein interactions (PPIs) remain underexplored. With the goal of contributing toward the expanded use of HP as a fundamental control parameter in protein research, processing, and engineering, small-angle X-ray scattering was used to examine the effects of HP and ionic strength on ovalbumin, a model protein. Based on an extensive data set, we develop an empirical method for scaling PPIs to a master curve by combining HP and osmotic effects. We define an effective pressure parameter that has been shown to successfully apply to other model protein data available in the literature, with deviations evident for proteins that do not follow the apparent Hofmeister series. The limitations of the empirical scaling are discussed in the context of the hypothesized underlying mechanisms.
Graphical abstract available at: https://doi.org/10.1021/acs.biomac.3c01001
Description
This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biomacromolecules, copyright © 2023 American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.biomac.3c01001. This article will be embargoed until 01/08/2025.
Keywords
chemical structure, protein structure, salts, scattering, x-ray scattering
Citation
Paul, Brian, Eric M. Furst, Abraham M. Lenhoff, Norman J. Wagner, and Susana C. M. Teixeira. “Combined Effects of Pressure and Ionic Strength on Protein–Protein Interactions: An Empirical Approach.” Biomacromolecules 25, no. 1 (January 8, 2024): 338–48. https://doi.org/10.1021/acs.biomac.3c01001.