Event Description
Title: Simulating Amyloid-β Folding under Confinement
Physics Major: Christopher Kepics
Abstract: Small aggregates of the Amyloid-β (Aβ) proteins have been implicated in the pathology of Alzheimer’s disease. The mechanisms of formation of these aggregates, however, is not known. A first step in understanding this problem is to examine how a single peptide misfolds into pathologic structures in biologically-relevant environments. To this end, in this study molecular dynamics computer simulations are used to examine how a fragment of the Aβ, the Aβ21−30, folds in a confined environment, mimicking cellular environments in vivo. This Aβ21−30 fragment is important because it has been identified as a folding nucleus for the full-length protein. Confinement is modeled by a spherical fullerene of adjustable size containing the Aβ21−30. This confinement limits the range of movement of the peptide favoring small conformational structures. By studying the Aβ21−30 under these conditions, our goal is to gain valuable insight into how confinement can affect the folding dynamics of the full-length protein.
Advisor: Dr. Luis Cruz Cruz
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