Dynamics of amyloid protein fibril elongation using isotope-labelled SANS
We will use SANS in combination with our new deuteration approach to investigate amyloid protein fibrils associated with diseases such as Alzheimers and prion disorders to give previously unavailable information in the linear growth rate of such fibrils. The approach involves placing deuterated "seeds" of protein fibrils in a contrast-matched deuterated solution, and then allowing these to grow in the presence of hydrogenated proteins. The hydrogenated proteins add to the growing ends of the fibrils, and this isotope labelling approach effectively allows us to only "see" these growing ends, which we can model as cylinders whose length increases with time. Such information is not available using any other solution technique; standard spectroscopic methods only give the overall % of protein in fibrillar vs non-fibrillar form, and the rate at which this changes, and cannot separate out the number (and length distribution) of fibrils, from the average rate at which each a single fibril grows. Such data are key to understanding the biological behavior of prion strains and other amyloid diseases, and is a prerequisite for further theoretical understanding of peptide fibrillization
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Adam M. Squires; EVES Ben; FORSYTH Victor Trevor; HAERTLEIN Michael; SCHWEINS Ralf and TERRY Ann. (2016). Dynamics of amyloid protein fibril elongation using isotope-labelled SANS. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-888
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