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Transformation of beta-sheet structures of the amyloid peptide induced by molecular modulators
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- 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 language | English |
|---|---|
| Journal | Chemical Communications |
| Volume | 50 |
| Issue | 64 |
| Pages (from-to) | 8923-8926 |
| Number of pages | 4 |
| ISSN | 1359-7345 |
| DOIs | |
| Publication status | Published - 18 Aug 2014 |
- SCANNING-TUNNELING-MICROSCOPY, ALZHEIMERS-DISEASE, FIBRIL FORMATION, CONFORMATIONS, CYTOTOXICITY, POLYPEPTIDES, AGGREGATION, ASSEMBLIES, DYNAMICS, BEHAVIOR
Research areas
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ID: 83191946