Ontology highlight
ABSTRACT:
SUBMITTER: Mao X
PROVIDER: S-EPMC3369759 | biostudies-literature | 2011 Jun
REPOSITORIES: biostudies-literature
Mao Xiaobo X Guo Yuanyuan Y Wang Chenxuan C Zhang Min M Ma Xiaojing X Liu Lei L Niu Lin L Zeng Qingdao Q Yang Yanlian Y Wang Chen C
ACS chemical neuroscience 20110330 6
The widely used method to monitor the aggregation process of amyloid peptide is thioflavin T (ThT) assay, while the detailed molecular mechanism is still not clear. In this work, we report here the direct identification of the binding modes of ThT molecules with the prion peptide GNNQQNY by using scanning tunneling microscopy (STM). The assembly structures of GNNQQNY were first observed by STM on a graphite surface, and the introduction of ThT molecules to the surface facilitated the STM observa ...[more]