X-ray analysis of amyloid-proteins using insulin as a model system
by
Gudrun Lotze, Institute for X-ray physics, University of Göttingen
→
Europe/Berlin
Bldg. 47c, room L109
Bldg. 47c, room L109
Description
Neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, and prion dis-
ease are caused by misfolding of the corresponding proteins. The folding process is accom-
panied by structural changes in the secondary protein structure, mainly due to conversion of
an alpha helix into a beta sheet conformation. It has long been known that insulin forms
amyloid fibrils if it is dissolved in acid solution (pH=2) and exposed to elevated temperature
(T>50 ◦C).
The results of a small-angle X-ray scattering analysis on the amyloid aggregation process
using insulin as model protein will be presented. The time dependency of different parameters
following a nucleation polymerization process will be shown. Furthermore, the special con-
centration dependency of the half time characterising the aggregation will be demonstrated.
