Monday, 23 May 2005
396

This presentation is part of: Spectroscopy of Biomolecules Posters

Formulating a Mechanism of Amyloid Growth using Single Molecule Spectroscopy

Jason T. Giurleo, Troy C. Messina, Hiyun Kim, Jongjin Jung, and David Talaga. Rutgers University, Piscataway, NJ

We are investigating the mechanism for the initial stages of protein self-assembly leading to amyloid growth using single molecule spectroscopy (SMS). B-lactoglobulin (b-LG) has been shown to form amyloid under denaturing conditions and has been chosen as a model protein for this study. Initial bulk experiments have been performed utilizing dynamic light scattering along with steady state and time-resolved fluorescence of conformationally sensitive fluorophores, and a preliminary mechanism of amyloid growth has been formulated. However, SMS has the potential to directly identify critical intermediates that could only be hypothesized by bulk experiments. A single molecule imaging experiment utilizing incubated samples of mono-labeled TMR-(b-LG) has been designed to count number of precursor monomers per aggregate species by counting the number of photobleaching steps required to extinguish a single particle's fluorescence. The time evolution of the particle number distribution is fit to a kinetic model representing a mechanism of amyloid growth.

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