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- W2056547829 abstract "Functional amyloids are found throughout nature as robust materials. We have discovered that template and adder proteins cooperatively self-assemble into micrometer-sized amyloid fibers with a controllable, hierarchical structure. Here, Escherichia coli is genetically engineered to express a template protein, Gd20, that can initiate self-assembly of large amyloid fibrils and fibers. Through atomic force microscopy (AFM) we found that expression of Gd20 produces large amyloid fibrils of 490 nm diameter and 2-15 μm length. Addition of an extracellular adder protein, myoglobin, continues self-assembly to form amyloid tapes with widths of ∼7.5 μm, heights of ∼400 nm, and lengths exceeding 100 μm. Without myoglobin the amyloid fibrils are metastable over time. When myoglobin is present, the amyloid fiber continues self-assembling to a width of ∼18 μm and height of ∼1 μm. Experimental results demonstrate that large amyloid fibers with a tailored stiffness and morphology can be engineered at the DNA level, spanning four orders of magnitude." @default.
- W2056547829 created "2016-06-24" @default.
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- W2056547829 date "2014-01-01" @default.
- W2056547829 modified "2023-10-01" @default.
- W2056547829 title "Genetically encoded self-assembly of large amyloid fibers" @default.
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- W2056547829 doi "https://doi.org/10.1039/c3bm60223k" @default.
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