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Equilibrium and kinetic studies of the counteraction of trehalose on acid-induced protein unfolding

Paper ID Volume ID Publish Year Pages File Format Full-Text
3459 171 2013 8 PDF Available
Title
Equilibrium and kinetic studies of the counteraction of trehalose on acid-induced protein unfolding
Abstract

It has been known that trehalose can counteract acid-induced protein denaturation and induce the formation of molten globule (MG) state, but the equilibrium and kinetic behaviors are still unclear. Herein, the counteraction of trehalose on the acid-induced unfolding of ferricytochrome c was studied at pH 2.0. Far-UV circular dichroism, Soret absorption and fluorescence spectra indicate that trehalose inhibits acid-induced protein denaturation and induces the formation of MG state. The kinetics of the counteracting effects of trehalose was investigated by stopped-flow fluorescence spectroscopy. It is found that the unfolding of ferricytochrome c displays three phases (i.e., fast, intermediate and slow phases) in the absence of trehalose. At trehalose <0.8 M, the unfolding transition still occurs in three phases, but at trehalose >0.8 M, it is transformed into a biphasic process without the fast phase. The rate constants for all the unfolding phases decrease linearly with increasing trehalose concentration. Meanwhile, the increase in the fluorescence intensity for the fast and intermediate phases diminishes with the increment of trehalose concentration. Nevertheless, there is little influence of trehalose on the fluorescence intensity change in the slow phase. The studies have provided new insight into the effects of trehalose on the stability of proteins.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Trehalose inhibits the acid-induced denaturation of ferricytochrome c at pH 2.0. ► Trehalose induces the formation of molten globule state at pH 2.0. ► At trehalose concentrations <0.8 M, the unfolding transition occurs in three phases. ► At trehalose concentrations >0.8 M, the unfolding transition occurs in two phases. ► The unfolding rates decrease linearly with increasing trehalose concentration.

Keywords
MG, molten globule state; N, native state; U, denatured state; I, intermediate state; Tris, tris(hydroxymethyl) aminomethane; HCl, hydrochloric acid; CD, circular dichroism; [θ]mrw, the mean residue ellipticity; [θ]obs, the observed circular dichroism sig
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Equilibrium and kinetic studies of the counteraction of trehalose on acid-induced protein unfolding
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 70, 15 January 2013, Pages 188–195
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us