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While our work in synthetic biology aims to design novel proteins that fold and function, our research on Alzheimer's disease attempts to understand how this debilitating neurodegenerative condition is caused when natural proteins misfold and malfunction. A specific protein fragment known as A-beta has a propensity to misfold and aggregate into clumps. These aggregates are toxic and cause a range of cellular and neurological symptoms. Our research uses a combination of chemical and genetic approaches to (a) understand the molecular determinants of this aggregation, and (b) discover novel compounds that inhibit aggregation. Such compounds may ultimately serve as leads towards the discovery of novel therapeutics to treat Alzheimer's disease.
The image at right is a collection of beta amyloid fibril pictures from "Mutations Enhance the Aggregation Propensity of the Alzheimer's Aβ Peptide" by Woojin Kim and Michael Hecht.