Single crystal X-ray diffraction studies of a terminally blocked tripeptide Boc-Leu(1)-Aib(2)-Leu(3)-OMe 1 demonstrates that it adopts a bend structure without any intramolecular hydrogen bond. Peptide 1 self-assembles to form a supramolecular antiparallel b-sheet structure by various non-covalent i
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Amyloid-like fibril-forming supramolecular β-sheets from a β-turn forming tripeptide containing non-coded amino acids: the crystallographic signature
✍ Scribed by Arijit Banerjee; Samir Kumar Maji; Michael G.B Drew; Debasish Haldar; Arindam Banerjee
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- French
- Weight
- 361 KB
- Volume
- 44
- Category
- Article
- ISSN
- 0040-4039
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The model tripeptide Boc-Leu(1)-Aib(2)-Phe(3)-OMe 1 containing a non-coded amino acid residue (Aib: a-amino isobutyric acid) forms a supramolecular helical assemblage via non-covalent interactions in single crystals. The SEM image of the peptide 1 in the solid state shows the ribbon like fibrillar m