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 Biotechnoljournal_title
Molecular biotechnologyauthors
Naik V,Kardani J,Roy Idoi
10.1007/s12033-016-9923-4subject
Has Abstractpub_date
2016-04-01 00:00:00pages
251-5issue
4eissn
1073-6085issn
1559-0305pii
10.1007/s12033-016-9923-4journal_volume
58pub_type
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