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

Authors

Peter Butko, University of Southern MississippiFollow
Justin P. Buford, University of Southern MississippiFollow
J. Shawn Goodwin, University of Southern MississippiFollow
Paul A. Stroud, University of Southern MississippiFollow
Charles L. McCormick, University of Southern MississippiFollow
Gordon C. Cannon, University of Southern MississippiFollow

Document Type

Article

Publication Date

1-12-2001

Department

Chemistry and Biochemistry

School

Mathematics and Natural Sciences

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

Recommended Citation

Butko, P., Buford, J. P., Goodwin, J. S., Stroud, P. A., McCormick, C. L., Cannon, G. C. (2001). Spectroscopic Evidence for Amyloid-like Interfacial Self-Assembly of Hydrophobin Sc3. Biochemical and Biophysical Research Communications, 280(1), 212-215.
Available at: https://aquila.usm.edu/fac_pubs/9166