Characterization of amyloidogenesis of hen egg lysozyme in concentrated ethanol solution
- Chemistry Department, Goucher College, 1021 Dulaney valley Road, Baltimore, MD 21204 (United States)
- Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205 (United States)
- Department of Physics, Astronomy and Geosciences, Towson University Nanotechnology Laboratory, Towson, MD 21252 (United States)
We show that hen egg white lysozyme [HEWL] reproducibly forms amyloid fibrils in 80% ethanol at 22 deg. C with constant agitation. Fibril formation occurs over a time course of approximately 30 days, displays polymerization nucleation kinetics, and demonstrates a marked decrease in {alpha}-helical structure. Seeding with as little as 0.05% v/v of fibrils cleaved into smaller seed fragments by sonication abolishes the lag phase. Thioflavin T assays confirm the amyloid nature of the fibrils. Atomic force microscopy reveals unbranched amyloid fibrils with lengths varying between 1 and 3 {mu}m and heights ranging from 6-12 nm. The formation of amyloid fibrils in predominantly organic solvents demonstrates that the basic principles guiding fibril formation arise from interactions of the peptide backbone rather than from interactions between the amino acid side chains.
- OSTI ID:
- 21143822
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 373, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2008.06.018; PII: S0006-291X(08)01144-3; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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