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Published online before print May 28, 2004, 10.1110/ps.03607204
Protein Science (2004), 13:1927-1932. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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FOR THE RECORD

Insulin forms amyloid in a strain-dependent manner: An FT-IR spectroscopic study

Wojciech Dzwolak1, Vytautas Smirnovas1, Ralf Jansen2 and Roland Winter2

1 High Pressure Research Center, Polish Academy of Sciences, 01-142 Warsaw, Poland
2 University of Dortmund, Department of Chemistry, Physical Chemistry I, D-44227 Dortmund, Germany

(RECEIVED December 27, 2003; FINAL REVISION March 9, 2004; ACCEPTED March 25, 2004)



Abstract

The presence of 20% (v/v) ethanol triggers growth of insulin amyloid with distinct infrared spectroscopic features, compared with the fibrils obtained under ambient conditions. Here we report that the two insulin amyloid types behave in the prion strain-like manner regarding seeding specificity and ability of the self-propagating conformational template to overrule unfavorable environmental factors and maintain the initial folding pattern. The type of the original seed has been shown to prevail over cosolvent effects and determines spectral position and width of the amide I' infrared band of the heterogeneously seeded amyloid. These findings imply that "strains" may be a common generic trait of amyloids.

Keywords: insulin; amyloid; prion strains; cross-seeding; protein aggregation

Abbreviations: FT-IR, Fourier transform infrared spectroscopy • AFM, atomic force microscopy • EtOD, d1-deuterated ethanol • HHBW, bandwidth at half height • BSE, bovine spongiform encephalopathy

Reprint requests to: Wojciech Dzwolak, High Pressure Research Center, Polish Academy of Sciences, Sokolowska 29/37, 01-142 Warsaw, Poland; e-mail: wdzwolak{at}unipress.waw.pl; fax: 48-22-632-42-18.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03607204.


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