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Soron következő előadás:

The role of supersaturation in aberrant protein aggregation
Yuji Goto (Institute for protein Research, Osaka University, Suita, Japan)


2012. augusztus 28. kedd 10 óra
ELTE TTK Lágymányosi campus, Déli Tömb 0.803 Szabó József terem

Kivonat:
Amyloid fibrils are associated with over 30 degenerative diseases including Alzheimer’s disease, and dialysis-related amyloidosis. To study amyloid fibrils, we developed two types of unique techniques.
First, we present that ultrasonication is one of the best means of accelerating amyloid nucleation and thus the formation of fibrils. Combining the use of ultrasonication and a microplate reader, we propose an efficient approach to studying the potential of proteins to form amyloid fibrils. The results indicate that the solutions of denatured proteins are often supersaturated above the solubility limit and ultrasonic agitations release the supersaturation effectively to form fibrils. We suggest that supersaturation of amyloidogenic proteins and peptides and its release by various biological factors explain the development of amyloidoses.
Second, to visualize amyloid fibrils, we combined total internal reflection fluorescence microscopy (TIRFM) with amyloid-specific thioflavin T (ThT) fluorescence. With this approach, we succeeded in observing the growth of amyloid fibrils in real-time at a single fibrillar level for various amyloidogenic proteins including A-beta peptide.
With these techniques, we compare the mechanisms of protein folding and misfolding. We propose a general view of how the structures of protein and peptide precipitates vary dramatically from single crystals to amyloid fibrils and amorphous aggregates, in which "solubility" and "supersaturation" play critical roles.

 

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