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Effects of osmolytes on protein-solvent interactions in crowded environment: Analyzing the effect of TMAO on proteins in crowded solutions.

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.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Breydo L,Sales AE,Ferreira L,Fedotoff O,Shevelyova MP,Permyakov SE,Kroeck KG,Permyakov EA,Zaslavsky BY,Uversky VN

doi

10.1016/j.abb.2015.02.021

subject

Has Abstract

pub_date

2015-03-15 00:00:00

pages

66-74

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(15)00083-1

journal_volume

570

pub_type

杂志文章

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