An amyloid-like fibril forming antiparallel supramolecular β-sheet from a synthetic tripeptide: a 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: 176 KB
• Volume: 44
• Category: Article
• ISSN: 0040-4039
• DOI: 10.1016/s0040-4039(03)01642-3

✦ Synopsis

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 interactions including intermolecular hydrogen bonds in the crystal and it exhibits amyloid-like fibrillar morphology in the solid state.