Amyloid fibrils are "alive": spontaneous refolding from one polymorph to another.
Mature fibrils prepared from apo-alpha-lactalbumin spontaneously refold from one polymorph to another as a result of a mild alteration in solution temperature and salinity. This discovery changes the very concept of the extraordinary stability of amyloid fibrils and presages a new approach for potentially regulating the biological activity of fibrils and their associated toxicity.
Kurouski
Dmitry
D
Department of Chemistry, University at Albany, SUNY, 1400 Washington Ave., Albany, NY 12222, USA.
Lauro
William
W
Lednev
Igor K
IK
D000682:Amyloid / Q000737:chemistry*; D001059:Apoproteins / Q000737:chemistry; D007768:Lactalbumin / Q000737:chemistry; D018625:Microscopy, Atomic Force; D017510:Protein Folding; D012965:Sodium Chloride / Q000737:chemistry; D013059:Spectrum Analysis, Raman; D013696:Temperature
D000682:Amyloid; D001059:Apoproteins; C041966:apo-alpha-lactalbumin; D012965:Sodium Chloride; D007768:Lactalbumin