Amyloid β (1-42) Folding Multiplicity and Single-Molecule Binding Behavior Studied with STM

Xiaojing Ma, Lei Liu, Xiaobo Mao, Lin Niu, Ke Deng, Weihui Wu, Yanmei Li, Yanlian Yang, Chen Wang

Research output: Contribution to journalArticlepeer-review


The fine folding and assembling characteristics of amyloid β (Aβ) peptides are important to pharmaceutical studies of drug molecules and to the pathological analysis of neurodegenerative disorders such as Alzheimer's disease at the molecular level. Here we present observations of the multiple folding characteristics of amyloid peptide Aβ42 lamellae using scanning tunneling microscopy. Molecularly resolved core regions of Aβ42 hairpins and unfolded peptide assembly structures are identified. The parallel assembling characteristics of Aβ42 hairpins can be confirmed in the study. In addition, single-molecule binding characteristics of Congo red and thioflavin T have been shown to bind at the groove regions of peptide assemblies. This study demonstrates a complementary venue for studying molecular heterogeneity of peptide assemblies, as well as the binding characteristics of molecular modulators.

Original languageEnglish (US)
Pages (from-to)894-901
Number of pages8
JournalJournal of molecular biology
Issue number4
StatePublished - May 15 2009
Externally publishedYes


  • STM
  • assembly structures
  • single-molecule binding behavior

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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