Spectroscopic Evidence for Amyloid-like Interfacial Self-Assembly of Hydrophobin Sc3
Chemistry and Biochemistry
Mathematics and Natural Sciences
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.
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