Surface charge patterns generated by atomic force microscopy-based charge writing were used to pattern amyloidlike peptide fibrils on a solid substrate. Fibrils of the short peptide TTR(105-115) were encapsulated inside water droplets of a water-in-perfluorocarbon oil emulsion and retained their rod morphology. They were observed to deposit selectively with a lateral resolution of approximately 1 mu m onto negatively charged patterns on a polymethyl-methacrylate substrate.
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