Patterning amyloid peptide fibrils by AFM charge writing.
Surface charge patterns generated by atomic force microscopy-based charge writing were used to pattern amyloid-like 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 microm onto negatively charged patterns on a polymethyl-methacrylate substrate.
Mesquida
Patrick
P
Department of Mechanical Engineering, King's College London, Strand, London WC2R 2LS, United Kingdom. patrick.mesquida@kcl.ac.uk
Blanco
E Macarena
EM
McKendry
Rachel A
RA