Journal
PROTEIN SCIENCE
Volume 13, Issue 7, Pages 1927-1932Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1110/ps.03607204
Keywords
insulin; amyloid; prion strains; cross-seeding; protein aggregation
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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.
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