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BP: Fachverband Biologische Physik

BP 7: Poster 1

BP 7.38: Poster

Monday, September 5, 2022, 18:00–20:00, P1

Observation of two-step aggregation kinetics of amyloid-β42 peptide from fractal analysis — •Soham Mukhopadhyay — Chair of Mathematics in Life Sciences, Friedrich-Alexander Universität Erlangen-Nürnberg, Cauerstr. 11, 91058 Erlangen, Germany — Max-Planck-Zentrum für Physik und Medizin, Erlangen, Germany

Proteins are responsible for controlling and catalyzing the reactions and processes that make life possible. Proper folding of protein molecules into their native states is critical for them to function correctly; conversely, misfolded proteins often cause damaging effects on the biological processes they are involved in. Misfolded proteins often undergo self-aggregation, a process that has been the subject of intense research due to its importance in biological contexts. Of particular interest is the formation of stable filamentous aggregates termed amyloids — implicated in the pathology of several diseases such as Alzheimer’s, Parkinson’s, type-II diabetes, etc. Several models propose a two-step aggregation mechanism, with linearly growing fibrils and branch formation through secondary growth.

In this work, we employ tools from fractal geometry to develop an analysis technique for images of protein aggregation obtained from TIRF microscopy. Fractal geometry provides an instinctive framework for analyzing 1- and 2-dimensional growth. We use this framework to study the aggregation of the amyloid-β42 peptide and find the initial aggregation to proceed in a one-dimensional fashion, with later branching events leading to two-dimensional growth. This provides direct evidence for the two-step aggregation model.