Binding modes of thioflavin T molecules to prion peptide assemblies identified by using scanning tunneling microscopy.
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 observations of the adsorption conformations of ThT with peptide strands. ThT molecules are apt to adsorb on the peptide assembly with β-sheet structure and oriented parallel with the peptide strands adopting four different binding modes. This effort could benefit the understanding of the mechanisms of the interactions between labeling species or inhibitory ligands and amyloid peptides, which is keenly needed for developing diagnostic and therapeutic approaches.
Key Laboratory for Biological Effects of Nanomaterials & Nanosafety and Key Laboratory of Standardization and Measurement for Nanotechnology (Chinese Academy of Sciences) National Center for Nanoscience and Technology, 11 Beiyitiao, Zhongguancun, Beijing 100190, P. R. China.
Xiaobo
X
Mao
Yuanyuan
Y
Guo
Chenxuan
C
Wang
Min
M
Zhang
Xiaojing
X
Ma
Lei
L
Liu
Lin
L
Niu
Qingdao
Q
Zeng
Yanlian
Y
Yang
Chen
C
Wang
D052160:Benzothiazoles; D016252:Microscopy, Scanning Tunneling / Q000379:methods; D011328:Prions / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D013844:Thiazoles / Q000737:chemistry / Q000378:metabolism*
D052160:Benzothiazoles; D011328:Prions; D013844:Thiazoles; C009462:thioflavin T