Literature DB >> 20132817

Recovery of functional enzyme from amyloid fibrils.

Gergely Agócs1, Katalin Solymosi, Andrea Varga, Károly Módos, Miklós Kellermayer, Péter Závodszky, Judit Fidy, Szabolcs Osváth.   

Abstract

Amyloid deposits, which accumulate in numerous diseases, are the final stage of multi-step protein conformational-conversion and oligomerization processes. The underlying molecular mechanisms are not fully understood, and particularly little is known about the reverse reaction. Here we show that phosphoglycerate kinase amyloid fibrils can be converted back into native protein. We achieved recovery with 60% efficiency, which is comparable to the success rate of the unfolding-refolding studies, and the recovered enzyme was folded, stable and fully active. The key intermediate stages in the recovery process are fibril disassembly and unfolding followed by spontaneous protein folding. Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2010        PMID: 20132817     DOI: 10.1016/j.febslet.2010.01.058

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase.

Authors:  Gergely Agócs; Bence T Szabó; Gottfried Köhler; Szabolcs Osváth
Journal:  Biophys J       Date:  2012-06-19       Impact factor: 4.033

2.  Distinct annular oligomers captured along the assembly and disassembly pathways of transthyretin amyloid protofibrils.

Authors:  Ricardo H Pires; Árpád Karsai; Maria J Saraiva; Ana M Damas; Miklós S Z Kellermayer
Journal:  PLoS One       Date:  2012-09-12       Impact factor: 3.240

3.  Protein aggregation profile of the human kinome.

Authors:  Ricardo Graña-Montes; Ricardo Sant'anna de Oliveira; Salvador Ventura
Journal:  Front Physiol       Date:  2012-11-20       Impact factor: 4.566

  3 in total

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