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 TTR105-115 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.