The Daily Bulletin

Paul Seidler, '05, '07, postdoctoral research fellow in molecular biology at UCLA, will present "Tau Protein Fibrils: Structure and Inhibition" at 12:30 p.m. Thursday, October 6, in Science and Mathematics Complex 170. This seminar series is sponsored by the Faculty-Student Association. An abstract of his talk appears below.

Abstract
The conversion of tau protein from a normal conformation to a pathological amyloid fold is highly correlated to the onset of Alzheimer’s disease (AD) and severity of cognitive decline. The overarching aim of my research is to develop methods and agents to block the formation and spread of toxic tau conformations. Using the atomic-resolution structure of the tau amyloid fiber core that I determined from nanocrystals using a new technique called microelectron diffraction, I am designing peptide-based inhibitors to halt tau amyloid fiber growth and spread. I am also pursuing an orthogonal inhibitor design strategy, which consists of studying protective mutations I've identified that are capable of suppressing tau assembly into toxic conformations. Using this approach, I hope to discover additional classes of evolutionarily-inspired tau inhibitors that will complement my structure-based design efforts.