Tracking protein aggregate interactions |
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Abstract: | Amyloid fibrils share a structural motif consisting of highly ordered β-sheets aligned perpendicular to the fibril axis1, 2. At each fibril end, β-sheets provide a template for recruiting and converting monomers3. Various amyloid fibrils often occur in the same individual, yet whether distinct protein aggregates aid or inhibit the assembly of heterologous proteins is unclear. In prion disease, different amyloid-like prion aggregate structures, or strains, are thought to be the basis of disparate disease phenotypes in the same species expressing identical prion protein sequences4-7. Here we focus on the interactions reported to occur when two pre-existing amyloids or two distinct prion strains occur together in the central nervous system. |
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