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Martin Carballo Pacheco, M.Sc.

Graduate Student/Coarse-grained Models of Amyloid Aggregation

Master's in Simulation Sciences, RWTH Aachen University (2013)

Location: Schinkelstrasse 2, Room 431a
Phone: +49 (0)241 80-99136

Amyloid fibrils are large protein aggregates. These aggregates are formed by peptides in a beta sheet conformation which lay perpendicular to the fibril axis. Amyloids have gained relevance in the scientific community as they have been found in the brains of patients with different neurodegenerative diseases, such as Alzheimer's and Parkinson's disease. However, in the last
years a series of amyloids, called functional amyloids, have been found with different normal physiological functions.

The discovery of functional amyloids has open many questions. One key question is to understand the reason for their lack of toxicity. Moreover, functional amyloids could
be used in the design of nanostructures. For example, a cytochrome can be added to an amyloid forming peptide to assemble nanowires. The goal of my thesis is to develop a fundamental understanding of functional amyloids using molecular simulations.
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Hypothetical aggregation model for the Aβ β-hairpin model. Figure from Hoyer et al., PNAS, 105, 5099 (2008). (Used for teaching purposes only.)