Trehalose-Induced Structural Transition Accelerates Aggregation of α-Synuclein.

Abstract:

:Fibrillation of α-synuclein proceeds through distinct stages, with oligomers combining to form the seed or the nucleus, followed by exponential and saturation phases. Osmolytes are considered to act as protein stabilizers by virtue of their ability to inhibit protein aggregation. Trehalose, a non-reducing disaccharide which is conventionally used as a stabilizer, was found to order α-synuclein, a natively disordered protein, into a non-native conformation such that the protein folding pathway is driven towards aggregation. Thus, by ordering the pathway intermediates, the osmolyte trehalose exerts variable effect on an intrinsically disordered protein when compared with its effect on natively folded proteins.

journal_name

Mol Biotechnol

journal_title

Molecular biotechnology

authors

Naik V,Kardani J,Roy I

doi

10.1007/s12033-016-9923-4

subject

Has Abstract

pub_date

2016-04-01 00:00:00

pages

251-5

issue

4

eissn

1073-6085

issn

1559-0305

pii

10.1007/s12033-016-9923-4

journal_volume

58

pub_type

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