(247b) The Effect of Halogenation of Erythrosine B on Amyloid-Beta 40 Oligomer Aggregation and Neurotoxicity in Alzheimer's Disease Using Molecular Modeling
- Conference: AIChE Annual Meeting
- Year: 2015
- Proceeding: 2015 AIChE Annual Meeting
- Group: Computational Molecular Science and Engineering Forum
Monday, November 9, 2015 - 6:00pm-8:00pm
Alzheimer’s disease (AD) is one of the most common type of degenerative dementia. Investigation on previous studies showed that the initial α-helical structure of the Aβ monomer formed an intermediate state of aggregation. Our collaborator Dr. Kwon observed that ER (Erythrosine B), a food dye approved by FDA, inhibited the formation of Aβ fibrils through in vitroexperiment. However, the mechanism of ER has not yet been discussed. In this study using molecular modeling methods such as docking and molecular dynamic simulations, the specific effect of modified ER on the Aβ40 monomer was explored by replacing the functional groups of ER. The effects of three modified ER drugs – ER, EOY and FLN – were studied by placing two of each drug on the two best binding sites then running GROMACS (4.6.1) with force field GROMOS96 to acquire analyses, such as RMSD, DSSP and SASA. ER and EOY interacted effectively with Aβ40 while the negative control FLN, modified ER without halogens, had little effect. Since it has been determined that halogens effectively inhibit aggregation of Aβ40, various concentrations of the modified ER drugs to find optimal inhibition results is to be studied.
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