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

abstract

• 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.

authors

• Kurouski, Dzmitry

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

publisher

• Elsevier  Publisher

published in

• Biochemical and Biophysical Research Communications  Journal

keywords

• Amyloid
• Animals
• Archaeal Proteins
• Cattle
• Chaperonin 60
• Insulins
• Kinetics
• Protein Structure, Secondary
• Proteolysis
• Pyrococcus Furiosus

PubMed Central ID

• 22564742

Digital Object Identifier (DOI)

• 10.1016/j.bbrc.2012.04.113

start page

• 97

end page

• 102

volume

• 422

issue

• 1

URL

• http://dx.doi.org/10.1016/j.bbrc.2012.04.113