Issue 46, 2023

Advances in protein solubility and thermodynamics: quantification, instrumentation, and perspectives

Abstract

While protein crystallization has broadly been applied to determine the 3D structure of proteins, it has recently drawn great attention to replace the traditional downstream processing for protein-based biopharmaceuticals due to its advantages in stability, storage, and delivery. However, establishing the crystallization conditions of a protein remains a challenge because of the limited understanding of the underlying phenomena. This highlight provides a critical review of the advanced experimental approaches to measure thermodynamic parameters (e.g. solubility) that can help in establishing the necessary conditions to perform a protein crystallization trial. Firstly, methods and techniques to assess protein crystallizability and solution quality are presented. Next, methodologies to measure the main thermodynamic parameters are revised (with the respective advantages, limitations, and studied proteins). Later, protocols and set-ups (with a focus on microfluidic devices) used to quantify solubility parameters are highlighted (involved apparatus capabilities, solubility screening details, and studied proteins). Lastly, future directions and outlook of this critical review are approached by covering new trends in the research field.

Graphical abstract: Advances in protein solubility and thermodynamics: quantification, instrumentation, and perspectives

Article information

Article type
Highlight
Submitted
28 Jul 2023
Accepted
10 Okt 2023
First published
11 Okt 2023
This article is Open Access
Creative Commons BY license

CrystEngComm, 2023,25, 6388-6404

Advances in protein solubility and thermodynamics: quantification, instrumentation, and perspectives

J. Ferreira and F. Castro, CrystEngComm, 2023, 25, 6388 DOI: 10.1039/D3CE00757J

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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