ACS Nano, 2016, doi: 10.1021/acsnano.5b07396
Niu L, Liu L, Xi W, Han Q, Li Q, Yu Y, Huang Q, Qu F, Xu M, Li Y, Du H, Yang R, Cramer J, Gothelf K V, Dong M, Besenbacher F, Zeng Q, Wang C, Wei G, Yang Y.
National Center for Nanoscience and Technology , Beijing 100190, China.
Institute for Advanced Materials, Jiangsu University , Jiangsu 212013, China.
Department of Physics, Fudan University , Shanghai 200433, China.
Department of Chemistry and iNANO, Center for DNA Nanotechnology, Aarhus University, Aarhus 8000, Denmark
Inhibition of amyloid aggregation is important for developing potential therapeutic strategies of amyloid-related diseases. Herein, we report that the inhibition effect of a pristine peptide motif (KLVFF) can be significantly improved by introducing a terminal regulatory moiety (terpyridine). The molecular-level observations by using scanning tunneling microscopy reveal stoichiometry-dependent polymorphism of the coassembly structures, which originates from the terminal interactions of peptide with organic modulator moieties and can be attributed to the secondary structures of peptides and conformations of the organic molecules. Furthermore, the polymorphism of the peptide-organic coassemblies is shown to be correlated to distinctively different inhibition effects on amyloid-β 42 (Aβ42) aggregations and cytotoxicity.