Combined Effects of Pressure and Ionic Strength on Protein–Protein Interactions: An Empirical Approach
| Author(s) | Paul, Brian | |
| Author(s) | Furst, Eric M. | |
| Author(s) | Lenhoff, Abraham M. | |
| Author(s) | Wagner, Norman J. | |
| Author(s) | Teixeira, Susana C. M. | |
| Date Accessioned | 2024-03-26T19:11:44Z | |
| Date Available | 2024-03-26T19:11:44Z | |
| Publication Date | 2024-01-08 | |
| 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. | |
| 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 | |
| Sponsor | This work was prepared under cooperative agreement #70NANB20H133 from NIST, U.S. Department of Commerce. We acknowledge the support of the National Institute of Standards and Technology, U.S. Department of Commerce, in providing the research facilities used in this work. This work utilized facilities supported in part by the National Science Foundation under Agreement No. DMR-0944772. We thank Jessie Hopkins and Max Watkins at the BioCAT beamline (APS) for useful discussions and guidance during data collection. The research used resources of the Advanced Photon Source, a US Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. BioCAT was supported by Grant P41 GM103622 from the National Institute of General Medical Sciences of the National Institutes of Health. Use of the Pilatus 3 1M detector was provided by Grant 1S10OD018090 from NIGMS. We thank Richard Gilillan and Qingqiu Huang at the HP Biobeamline (CHESS) for useful discussions and guidance during data collection. Research conducted at the Center for High-Energy X-ray Sciences (CHEXS) is supported by the National Science Foundation (BIO, ENG and MPS Directorates) under award DMR-1829070, and the Macromolecular Diffraction at CHESS (MacCHESS) facility, which is supported by award 1-P30-GM124166-01A1 from the National Institute of General Medical Sciences, National Institutes of Health, and by New York State’s Empire State Development Corporation (NYSTAR). This work benefitted from use of the SasView software, which was originally developed by the DANSE project under NSF Award DMR-0520547. Certain instruments and software are identified to foster understanding. Such identification does not imply recommendation or endorsement by the National Institute of Standards and Technology, nor does it imply that the instruments and software identified are necessarily the best available for the purpose. The statements, findings, conclusions and recommendations are those of the authors and do not necessarily reflect the view of NIST, the National Institute of General Medical Sciences, the National Institutes of Health, or the U.S. Department of Commerce. | |
| 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. | |
| ISSN | 1526-4602 | |
| URL | https://udspace.udel.edu/handle/19716/34226 | |
| Language | en_US | |
| Publisher | Biomacromolecules | |
| Keywords | chemical structure | |
| Keywords | protein structure | |
| Keywords | salts | |
| Keywords | scattering | |
| Keywords | x-ray scattering | |
| Title | Combined Effects of Pressure and Ionic Strength on Protein–Protein Interactions: An Empirical Approach | |
| Type | Article |
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