Rapid degradation kinetics of amyloid fibrils under mild conditions by an archaeal chaperonin. Academic Article uri icon


  • Amyloid depositions containing exceptionally stable -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 -sheet is quickly transformed into a mix of -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.

published proceedings

  • Biochem Biophys Res Commun

author list (cited authors)

  • Kurouski, D., Luo, H., Sereda, V., Robb, F. T., & Lednev, I. K.

citation count

  • 19

complete list of authors

  • Kurouski, Dmitry||Luo, Haibin||Sereda, Valentin||Robb, Frank T||Lednev, Igor K

publication date

  • January 2012