Recovery of functional enzyme from amyloid fibrils |
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Authors: | Gergely Agó cs,Andrea Varga,Mikló s Kellermayer,Judit Fidy |
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Affiliation: | a Department of Biophysics and Radiation Biology, Semmelweis University, T?zoltó u. 37-47, H-1094 Budapest, Hungary b Department of Plant Anatomy, Eötvös Loránd University, Pázmány Péter s. 1/C, H-1117 Budapest, Hungary c Institute of Enzymology, Biological Research Center, Karolina út 29, H-1113 Budapest, Hungary |
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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. |
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Keywords: | PGK, yeast (Saccharomyces cerevisiae) phosphoglycerate kinase 3-PG, 3-phosphoglycerate |
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