Presentation Title

Brownian Dynamics Simulations of Amyloid Beta-42 Protein Aggregation​

Faculty Mentor

Timothy Cholko, Chia-en Chang

Start Date

23-11-2019 8:00 AM

End Date

23-11-2019 8:45 AM

Location

235

Session

poster 1

Type of Presentation

Poster

Subject Area

physical_mathematical_sciences

Abstract

Brownian Dynamic(BD) simulations of protein-protein interactions provides information that may help characterize aggregation mechanisms which lead to toxic fibril formation. This research focuses on amyloid beta 42(AB42) proteins which, when aggregated, are hypothesized to be a contributing factor to the neurodegenerative effects of Alzheimer's Disease(AD). One of the main goals in this work is to understand how these proteins interact with one of four self-assembling monolayers(SAMs) and how these interactions can affect the aggregation process, whether that be by speeding up the stacking of proteins or by slowing it down. Each SAM has a varying group with either a CH3, OH, NH2, and COO surface to model hydrophobic, hydrophilic, positively charged, and negatively charged surfaces, respectively. In addition to these four simulations there is also an AB42 dimer simulation being run without a SAM as a standard to which we can compare results. The data gained from the GeomBD simulations is analyzed with programs that are already a part of GeomBD, or other programs that need to be written in order to analyze the data obtained from GeomBD to get more information on the interactions occurring. If a full understanding of these mechanisms can be reached, then there may be many applications to drug designs aimed at inhibiting such aggregations.

This document is currently not available here.

Share

COinS
 
Nov 23rd, 8:00 AM Nov 23rd, 8:45 AM

Brownian Dynamics Simulations of Amyloid Beta-42 Protein Aggregation​

235

Brownian Dynamic(BD) simulations of protein-protein interactions provides information that may help characterize aggregation mechanisms which lead to toxic fibril formation. This research focuses on amyloid beta 42(AB42) proteins which, when aggregated, are hypothesized to be a contributing factor to the neurodegenerative effects of Alzheimer's Disease(AD). One of the main goals in this work is to understand how these proteins interact with one of four self-assembling monolayers(SAMs) and how these interactions can affect the aggregation process, whether that be by speeding up the stacking of proteins or by slowing it down. Each SAM has a varying group with either a CH3, OH, NH2, and COO surface to model hydrophobic, hydrophilic, positively charged, and negatively charged surfaces, respectively. In addition to these four simulations there is also an AB42 dimer simulation being run without a SAM as a standard to which we can compare results. The data gained from the GeomBD simulations is analyzed with programs that are already a part of GeomBD, or other programs that need to be written in order to analyze the data obtained from GeomBD to get more information on the interactions occurring. If a full understanding of these mechanisms can be reached, then there may be many applications to drug designs aimed at inhibiting such aggregations.