Probing phospholipid induced α-synuclein aggregation with tryptophan fluorescence

PHYS 336

Candace M. Pfefferkorn, pfefferc@mail.nih.gov and Jennifer C. Lee, leej4@mail.nih.gov. Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, 9000 Rockville Pike, National Institutes of Health, Bethesda, MD 20892
Understanding the environmental factors affecting the aggregation of α-synuclein (α-syn) is of great importance because the accumulation and deposit of α-syn are intimately connected to Parkinson's disease etiology. In the current study, synthetic phospholipid vesicles are employed as membrane mimics to investigate the mechanism of bilayer induced fibril formation. A single tryptophan mutation was incorporated into five different sites (W4, W39, W94, W125, W136) to serve as fluorescent probes of distinct regions of the protein. Measurements of steady-state and time-resolved fluorescence are employed to monitor protein-membrane interactions and membrane stimulated protein aggregation.
 

PHYS Poster Session - Optical Probes of Dynamics in Complex Environments
7:30 PM-10:00 PM, Wednesday, April 9, 2008 Morial Convention Center -- Hall A, Poster

Sci-Mix
8:00 PM-10:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Sci-Mix

Division of Physical Chemistry

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008