Title

Spectroscopic Evidence for Amyloid-like Interfacial Self-Assembly of Hydrophobin Sc3

Document Type

Article

Publication Date

1-12-2001

Department

Chemistry and Biochemistry

Abstract

Amphipathic fungal proteins called hydrophobins are able to self-assemble into insoluble supramolecular structures at hydrophobic/hydrophilic interfaces, but the molecular mechanism and underlying protein conformation changes are not known. Secondary-structure prediction indicated that hydrophobin Sc3 is an all-β protein. Many amyloidogenic proteins self-assemble into insoluble amyloid fibrils while undergoing a change to an all-β conformation. In this study we show that two dyes, thioflavin T, and Congo red, which are widely used for specific detection of stacked β sheets, interact with Sc3 assemblies in the same way as with the amyloid β-sheet fibrils. We conclude that Sc3, and probably other hydrophobins too, self-assemble at interfaces in the same manner as amyloidogenic proteins, i.e., through β-sheet stacking.

Publication Title

Biochemical and Biophysical Research Communications

Volume

280

Issue

1

First Page

212

Last Page

215

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