Date: 17.11.2023, Time: 15:30h

Location: Kleiner Physikhörsaal N020, Faculty of Physics
The talk will also be streamed online.

Prof. Roland Riek
ETH Zürich

Amyloids are well known from their association to Alzheimer's disease and other neurodegenerative diseases. They are composed of a highly ordered repetitive inter-molecular beta-sheet structure composed of many thousands copies of a given protein or peptide. They are very stable under harsh conditions, can growth like a one dimensional crystal and already dipeptides are able to form this particular structure. Based on these findings, it was rationalized that peptide amyloids may have played important roles in the prebiotic world.
Indeed, peptide amyloids can be catalytically active. Peptide amyloids form spontaneously under prebiotic conditions upon peptide condensation from amino acids in presence of COS gas. Peptide amyloids are chiral-selective. Peptide amyloids can chemically replicate themselves by template assistance. Peptide amyloids stabilize RNA molecules and vice versa RNA molecule stabilize peptide amyloids. The peptide amyloid- RNA interactions are somewhat specific and show nM affinity attributed to avidity. Interestingly, significant binding requests codon sized tri-nucleotides opening the hypothesis that the amyloid-RNA interaction played a role in the genetic code evolution.
Peptide amyloids are synthesized inside fatty acid vesicles starting from activated amino acids in the solvent. Peptide amyloids can bind ATP in a canonical fashion representing an ancient ATP binding stie in contrast to ADP. The known proteome comprises an amyloid over population. The reader is invited to join the science around the peptide amyloid world hypothesis.