Spectroscopic Evidence for Amyloid-like Interfacial Self-Assembly of Hydrophobin Sc3
Chemistry and Biochemistry
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-beta protein. Many amyloidogenic proteins self-assemble into insoluble amyloid fibrils while undergoing a change to an all-beta conformation. In this study we show that two dyes, thioflavin T, and Congo red, which are widely used for specific detection of stacked beta sheets, interact with Sc3 assemblies in the same way as with the amyloid beta -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 beta -sheet stacking. (C) 2001 Academic Press.
Biochemical and Biophysical Research Communications
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