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Published online before print January 10, 2004, 10.1110/ps.03183404
Protein Science (2004), 13:319-324. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Formation of amyloid fibrils from fully reduced hen egg white lysozyme

Aoneng Cao, Daoying Hu and Luhua Lai

State Key Laboratory of Structural Chemistry for Stable and Unstable Species, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, People’s Republic of China

(RECEIVED May 2, 2003; FINAL REVISION October 10, 2003; ACCEPTED October 16, 2003)



Abstract

The fully reduced hen egg white lysozyme (HEWL), which is a good model of random coil structure, has been converted to highly organized amyloid fibrils at low pH by adding ethanol. In the presence of 90% (v/v) ethanol, the fully reduced HEWL adopts {beta}-sheet secondary structure at pH 4.5 and 5.0, and an {alpha}-to-{beta} transition is observed at pH 4.0. A red shift of the Congo red absorption spectrum caused by the precipitation of the fully reduced HEWL in the presence of 90% (v/v) ethanol is typical of the presence of amyloid aggregation. EM reveals unbranched fibrils with a diameter of 2–5 nm and as long as 1–2 µm. The pH dependence of the initial structure of the fully reduced HEWL in the presence of 90% (v/v) ethanol suggests that Asp and His residues may play an important role.

Keywords: Amyloid fibril formation; hen lysozyme; disulfide reduction

Abbreviations: HEWL, hen egg white lysozyme • DTTred, reduced DL-dithiothreitol • TFE, trifluoroethanol • CD, circular dichroism • CR, congo red • GdHCl, guanidine hydrochloride • AEMTS, 2-aminoethyl methanethiosulfonate • EDTA, ethylenediaminetetraacetic acid • Tris-HCl, tris (hydroxymethyl) aminomethane hydrochloride

Reprint requests to: Luhua Lai, College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, People’s Republic of China; e-mail: lhlai{at}pku.edu.cn; fax: 86-10-62751725.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03183404.


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