Journal
ACS NANO
Volume 10, Issue 4, Pages 4143-4153Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsnano.5b07396
Keywords
amyloid beta (A beta) peptide; scanning tunneling microscopy; peptide aggregation; peptide motif; polymorphism effect; amyloid cytotoxicity; inhibitory effect
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Funding
- National Natural Science Foundation of China [91127043, 21261130090, 21273051, 21573097]
- Sino-Danish Center
- Youth Natural Science Foundation of Jiangsu Province [BK20130493]
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Inhibition of amyloid aggregation is important for developing potential therapeutic strategies of amyloidrelated 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-beta 42 (A beta 42) aggregations and cytotoxicity.
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