Efficient conversion of intact hen lysozyme into amyloid fibrils by seeding

Content Provider	Semantic Scholar
Author	Sasaki, Ken Nakatsuka, Ken Hayashi, Itsuho
Copyright Year	2008
Abstract	Clarifying the mechanism how intact protein is transformed into amyloid fibrils has central importance in the study of amyloidosis. When hen lysozyme is kept in an acidic solution (pH 2.2, 80 mM NaCl) at a temperature close to its transition temperature (e.g., 57 oC), amyloid fibrils are formed after a lag-time of several to 11 days. These fibrils are mainly composed of peptide fragments produced by acid-degradation of the protein at selective Asp-Gly sites (Mishra et al., J. Mol. Biol. 366, 1029-1044, 2007). We found that, when these fibrils are sonicated into small particles and a fraction is mixed into a solution of fresh intact hen lysozyme (pH 2.2, 80 mM NaCl), the second-generation amyloid fibrils are rapidly formed from the intact protein in an apparent two-state manner. The rate of the fibril formation depends critically on temperature in the transition region, showing that the fibrillation formation initiates by the interaction of the seed with heat-denatured protein. The efficient conversion of α-rich monomer proteins into β-rich amyloid fibrils by seeding with preformed fibrils could be part of a general mechanism of amyloid fibril formation and infection in vivo.
Starting Page	11
Ending Page	18
Page Count	8
File Format	PDF HTM / HTML
Volume Number	8
Alternate Webpage(s)	http://www.jsb.gr.jp/jbm/2008/0801_2.pdf
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article