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March 12, 2012

Speaker: Dr. Steven Johnson, University of Washington, Seattle, Washington

Title: Medicinal chemistry strategies for modulating protein (mis)folding pathways associated with human diseases

Abstract: Proteins need to be properly folded in order to perform their functions. As such, cells have evolved biochemical pathways to help ensure that proteins either fold properly or are targeted for degradation. Nonetheless, there are instances where these systems fail, allowing misfolded proteins to accumulate, often with pathological consequences. Transthyretin, for example, can be prone to amyloidogenesis, the process of protein misfolding and subsequent aggregation, which is implicated in several human diseases. One therapeutic strategy for such maladies is to directly target the folded protein with a small molecule native state stabilizer, thereby inhibiting amyloidogenesis. Another, potentially far reaching strategy to address protein (mis)folding pathways, is to target molecular chaperones, cellular machines specialized in helping proteins fold properly. I will present my research on both avenues highlighting the application of structure activity relationships, medicinal chemistry, and high throughput screening for the discovery and development of novel small molecule probes and therapeutics for modulating protein (mis)folding pathways.

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