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Time

Friday 28 February 2014, at 10:15 - 11:00

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Location

The auditorium of the iNANO House (1593-012), Gustav Wieds Vej 14, 8000 Aarhus C

By Trine Møller Hansen

Director Vinod Subramaniam, FOM Institute AMOLF, Amsterdam, The Netherlands

Amyloid at the nanoscale

Misfolding and aggregation of proteins into nanometer-scale fibrillar assemblies, called amyloid, is a hallmark of many neurodegenerative diseases. On the other hand, amyloid nanostructures also have functional roles, such as in bacterial adhesion and in the glue of barnacles. Although vastly different proteins can form structurally similar amyloid nanostructures, the underlying biophysical principles are incompletely understood. We have extensively investigated the self-assembly of the human alpha-synuclein protein, involved in Parkinson’s disease, into amyloid fibrils. A particularly relevant question is the role of early oligomeric aggregates in modulating the dynamics of protein nucleation and aggregation, and in membrane interactions. In this talk, I will summarize work using single molecule fluorescence spectroscopy to gain insights into the structure and composition of oligomeric aggregates of the protein, and the interaction of these oligomers with lipid membranes. If time permits, I will give a glimpse into quantitative atomic force microscopy and nanomechanical investigations that provide information on amyloid fibril polymorphism and on nanoscale mechanical properties of mature fibrillar species

Host: Professor Daniel Otzen, iNANO & Department of Molecular Biology and Genetics, Aarhus University, Aarhus

Coffee, tea and bread will be served in front of the iNANO auditorium from 10:00.

Distinguished iNANO Lecture: Amyloid at the nanoscale

Info about event

Time

Location

Director Vinod Subramaniam, FOM Institute AMOLF, Amsterdam, The Netherlands

Amyloid at the nanoscale