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

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

  • Lin Niu, Chinese Acad Sci, Chinese Academy of Sciences, Inst High Energy Phys, Key Lab Biomed Effects Nanomat & Nanosafety
  • ,
  • Lei Liu, Chinese Acad Sci, Chinese Academy of Sciences, Inst High Energy Phys, Key Lab Biomed Effects Nanomat & Nanosafety, Institute for Advanced Materials, Jiangsu University, Denmark
  • Meng Xu, Chinese Acad Sci, Chinese Academy of Sciences, Inst High Energy Phys, Key Lab Biomed Effects Nanomat & Nanosafety
  • ,
  • Jacob Cramer, Denmark
  • Kurt V. Gothelf
  • MD Dong
  • Flemming Besenbacher
  • Qingdao Zeng, Chinese Acad Sci, Chinese Academy of Sciences, Inst High Energy Phys, Key Lab Biomed Effects Nanomat & Nanosafety
  • ,
  • Yanlian Yang, Chinese Acad Sci, Chinese Academy of Sciences, Inst High Energy Phys, Key Lab Biomed Effects Nanomat & Nanosafety
  • ,
  • Chen Wang, Chinese Acad Sci, Chinese Academy of Sciences, Inst High Energy Phys, Key Lab Biomed Effects Nanomat & Nanosafety, Unknown
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

    Research areas

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

See relations at Aarhus University Citationformats

ID: 83191946