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Putting the Piezolyte Hypothesis under Pressure.

Christina M Papini¹, Pranav P Pandharipande², Catherine A Royer¹

¹Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York; Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, New York.

Biophysical Journal

|August 15, 2017

Summary

This summary is machine-generated.

Small molecules stabilizing proteins under high pressure, termed piezolytes, do not directly affect protein volume changes upon unfolding. This study indicates these compounds cannot be classified as piezolytes based on volumetric properties.

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Area of Science:

Biochemistry
Protein Science
Physical Chemistry

Background:

Piezolytes are stabilizing cosolutes that counteract high hydrostatic pressure effects on proteins.
This classification implies piezolytes influence protein volumetric properties.

Discussion:

This study investigated the volumetric effects of proposed piezolytes (glutamate, sarcosine, betaine) on model proteins (lysozyme, ribonuclease A).
Differential scanning calorimetry and pressure perturbation calorimetry were used to measure changes in thermostability and volume upon unfolding.
Results showed increased protein stability and transition temperature with increasing cosolute concentration, but no change in the temperature dependence of unfolding volume changes.

Key Insights:

Proposed piezolytes do not alter the temperature dependence of protein unfolding volume changes.
The direct impact of these cosolutes on protein volumetric properties under pressure was not observed.
The findings challenge the classification of glutamate, sarcosine, and betaine as piezolytes based on volumetric mechanisms.

Outlook:

Further research is needed to explore alternative mechanisms for pressure stabilization by these cosolutes.
Investigating other types of cosolutes and their volumetric effects under pressure is warranted.
Understanding the precise molecular interactions governing protein stability under hydrostatic pressure remains a key area for future studies.