Recovery of functional enzyme from amyloid fibrils

Gergely Agócs, K. Solymosi, A. Varga, K. Módos, M. Kellermayer, P. Závodszky, J. Fidy, Szabolcs Osváth

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1139-1142
Number of pages4
JournalFEBS Letters
Volume584
Issue number6
DOIs
Publication statusPublished - Mar 2010

Fingerprint

Amyloid
Phosphoglycerate Kinase
Protein folding
Recovery
Oligomerization
Protein Folding
Amyloid Plaques
Enzymes
Proteins
Deposits

Keywords

  • Amyloid
  • Enzyme activity
  • Protein aggregation
  • Refolding

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Cite this

Recovery of functional enzyme from amyloid fibrils. / Agócs, Gergely; Solymosi, K.; Varga, A.; Módos, K.; Kellermayer, M.; Závodszky, P.; Fidy, J.; Osváth, Szabolcs.

In: FEBS Letters, Vol. 584, No. 6, 03.2010, p. 1139-1142.

Research output: Contribution to journalArticle

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