Linked dimeric ß-barrel yields stable oligomers that resemble amyloid intermediates

MARIANO DELLAROLE; IGNACIO E. SANCHEZ; GONZALO DE PRAT GAY

SAN DIEGO, USA

Simposio; 22nd Annual Symposium of The Protein Society. Proteins: Machines of Life; 2008

The C-terminal homodimeric domain of the human papillomavirus type 16 E2 protein forms amyloid fibrils under mildly denaturing conditions. We have used a single chain variant of thedomain (scE2C) to gain insight into the mechanism of misfolding. We combine circular dichroism, dynamic light scattering, amyloid binding dyes, atomic force microscopy and kinetic measurements to elucidate the polymerization mechanism and morphology of the products. Could monomerized variants be a tool for investigating the mechanisms of amyloidogenesis?