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Observation of sequence specificity in the seeding of protein amyloid fibrils
Authors:Krebs Mark R H  Morozova-Roche Ludmilla A  Daniel Katie  Robinson Carol V  Dobson Christopher M
Affiliation:Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Abstract:It is well established that the rate of formation of fibrils by amyloidogenic proteins is enhanced by the addition of preformed fibrils, a phenomenon known as seeding. We show that the efficiency of seeding fibril formation from solutions of hen lysozyme by a series of other proteins depends strongly on the similarity of their sequences. This observation is consistent with the importance of long-range interactions in stabilizing the core structure of amyloid fibrils and may be associated with the existence of a species barrier observed in the transmissible spongiform encephalopathies. In addition, it is consistent with the observation of a single dominant type of protein in the deposits associated with each form of amyloid disease.
Keywords:amyloid   lysozyme   seeding   cross-seeding   species barrier
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