Abstract

One of the most intriguing issues in biology is the occasional conversion of proteins from their folded functional forms into thread-like molecular aggregates designated as amyloids. These transformations into an alternative form of protein structure are linked to over 40 pathological conditions ranging from neurodegenerative disorders to systemic amyloidoses. Besides their feared pathological nature, amyloids represent an appealing target for many research disciplines including Material Science,Biotechnology and Chemistry.

The seminar will focus on two amyloidogenic systems. In the case of class I hydrophobins, the self-assembly into polymers sharing large similarities with amyloids is functional and allows for the formation of water-repellent monolayers on the surface of structures such as spores and fruiting bodies. In the case of acylphosphatase, specific conditions promote an accidental aggregation into amyloids via mechanisms typical of the processes occurring in vivo at the insurgence of amyloid diseases.

Combined approaches of experiments and multiscale simulations have been employed to point out the intimate connection between protein dynamics and self-assembly. The data will show how subtle variations in the conformational free energy of protein monomers govern the processes leading to amyloid formation.