Transformation of beta-sheet structures of the amyloid peptide induced by molecular modulators

Lin Niu, Lei Liu, Meng Xu, Jacob Cramer, Kurt V. Gothelf, MD Dong, Flemming Besenbacher, Qingdao Zeng, Yanlian Yang*, Chen Wang

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Abstract

In this work we report the effect of terminus molecular modulators on the secondary structures of the amyloid peptide aggregates. The controlled modulation of the assembly structure and the transformation of beta-sheet secondary structures could be beneficial for gaining insight into the aggregation mechanism of peptides. Particularly, multiple assembling characteristics have been identified as a reflection of peptide-organic interactions.
Original languageEnglish
JournalChemical Communications
Volume50
Issue64
Pages (from-to)8923-8926
Number of pages4
ISSN1359-7345
DOIs
Publication statusPublished - 18 Aug 2014

Keywords

  • SCANNING-TUNNELING-MICROSCOPY
  • ALZHEIMERS-DISEASE
  • FIBRIL FORMATION
  • CONFORMATIONS
  • CYTOTOXICITY
  • POLYPEPTIDES
  • AGGREGATION
  • ASSEMBLIES
  • DYNAMICS
  • BEHAVIOR

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