Binding modes of thioflavin T molecules to prion peptide assemblies identified by using scanning tunneling microscopy

Xiaobo Mao, Yuanyuan Guo, Chenxuan Wang, Min Zhang, Xiaojing Ma, Lei Liu, Lin Niu, Qingdao Zeng, Yanlian Yang, Chan Wang

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)281-287
Number of pages7
JournalACS Chemical Neuroscience
Volume2
Issue number6
DOIs
StatePublished - Jun 15 2011

Keywords

  • GNNQQNY
  • amyloid
  • binding mode
  • labeling molecule
  • scanning tunneling microscopy
  • thioflavin T

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Cognitive Neuroscience
  • Cell Biology

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