Alzheimer disease is the one of the most common form of degenerative dementia. There is no cure for the disease and current treatments only help with the symptoms of the disease. As a main cause of the disease, the formation of neurotoxic plaque composed of 39 to 42 residue-long amyloid beta (A�) fibril has been found in the patient's brain with relatively high portion. Through a series of investigation about the mechanism of beta amyloid aggregation, it was found that initial A� monomer undergoes intermediate state for aggregation so-called aggregation-prone state (APS) which is partially folded.Erythrosine B (ER) is one of the prominent drug candidates to impede the aggregation of the A� peptides. ER is a common xanthene dye approved not having any toxicity to humans under daily dose of 60 mg/kg and generates fragmented A� fibrils and protofibrils. As a collaboration work, the effect of ER on the Amyloid beta monomer has been suggested as an inhibitor of fibril elongation through in vitro experiment.In this study using molecular modeling methods such as docking and molecular dynamics simulation, the specific effect of modified ER on A�40 monomer will be investigated by replacing the functional group of ER.

Investigation of the effect of the modified erythrosin B on amyloid beta 40 monomer using molecular modeling

248th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.