Rapid degradation kinetics of amyloid fibrils under mild conditions by an archaeal chaperonin

Biochemical and Biophysical Research Communications
Dmitry KurouskiIgor K Lednev

Abstract

Amyloid depositions containing exceptionally stable β-sheet rich protein aggregates, called fibrils are associated with prevalent and incurable neurodegenerative diseases. Chaperones are proteins that facilitate protein folding in both eukaryotes and prokaryotes. We found that a cold-adapted mutant ATP-dependant chaperonins (Hsp60) from a hyperthermophilic archaeon binds to and fragments insulin fibrils very rapidly with local targeted entry points. Individual fragments swell and the fibrillar β-sheet is quickly transformed into a mix of α-helical and unordered protein structures. After further incubation, the fragments coalesced, forming large amorphous aggregates with poly-disperse topologies. This finding represents a new approach to the disassembly of refractory protein aggregates under physiological conditions.

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Citations

Jun 7, 2016·Journal of Dairy Science·Hong-Hua XuJun-Yan Tan
Dec 21, 2016·Biochemistry·Madhavi Kanuru, Gopala Krishna Aradhyam
Aug 26, 2015·The EMBO Journal·Nava ZaarurMichael Y Sherman
Dec 30, 2014·The Journal of Physical Chemistry. B·Manuel F Rosario-AlomarIgor K Lednev

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