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Review
. 2019 Fall;18(Suppl1):13-30.
doi: 10.22037/ijpr.2020.112621.13857.

Osmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization

Somayeh Mojtabavi  1   2 , Nasrin Samadi  2 , Mohammad Ali Faramarzi  1
Affiliations
Review

Osmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization

Somayeh Mojtabavi et al. Iran J Pharm Res. 2019 Fall.

Abstract

It is well-known that the typical protein's three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules typically called "compatible" solutes, based on the concept that they do not perturb cellular components. However, urea and guanidine hydrochloride (GuHCl) as denaturing osmolytes destabilize many macromolecular structures and inhibit functions. Several studies have been so far performed to explain the actual interaction of an osmolyte with a protein. The present review is aimed to achieve a collective knowledge of the progress arise in the field of osmolyte-protein interactions. The following is also an overview of the main techniques to measure protein stability in the presence of osmolytes.

Keywords: Folding state; Osmolyte; Preferential hydration; Protein stability; Protein structure.

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Figures

Figure 1
Figure 1
Chemical structures of the most common osmolytes belonging to (a) methylamine and (b) amino acid classes
Figure 2
Figure 2
Chemical structures of osmolytes classified in polyols
Figure 3
Figure 3
Chemical structures of the miscellaneous group of osmolytes
Figure 4
Figure 4
Schematic representation of the preferential exclusion of a compatible osmolyte on protein under stress conditions
Figure 5
Figure 5
The mechanism and thermodynamic effects of stabilization and destabilization of a protein in the presence of osmo-protectants and denaturants
See this image and copyright information in PMC

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