Effects of Osmolytes on Protein-solvent Interactions in Crowded Environment: Analyzing the Effect of TMAO on Proteins in Crowded Solutions

Document Type

Article

Publication Date

2015

Keywords

Partitioning, Macromolecular crowding, Protein structure, Protein stability, Aqueous two-phase system, Structural changes, Solvent interaction analysis

Digital Object Identifier (DOI)

https://doi.org/10.1016/j.abb.2015.02.021

Abstract

We analyzed the effect of a natural osmolyte, trimethylamine N-oxide (TMAO), on structural properties and conformational stabilities of several proteins under macromolecular crowding conditions by a set of biophysical techniques. We also used the solvent interaction analysis method to look at the peculiarities of the TMAO-protein interactions under crowded conditions. To this end, we analyzed the partitioning of these proteins in TMAO-free and TMAO-containing aqueous two-phase systems (ATPSs). These ATPSs had the same polymer composition of 6.0 wt.% PEG-8000 and 12.0 wt.% dextran-75, and same ionic composition of 0.01 M K/NaPB, pH 7.4. These analyses revealed that there is no direct interaction of TMAO with proteins, suggesting that the TMAO effects on the protein structure in crowded solutions occur via the effects of this osmolyte on solvent properties of aqueous media. The effects of TMAO on protein structure in the presence of polymers were rather complex and protein-specific. Curiously, our study revealed that in highly concentrated polymer solutions, TMAO does not always act to promote further protein folding.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Archives of Biochemistry and Biophysics, v. 570, p. 66-74

Link to Full Text

Share

COinS