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An amyloid-like fibril forming antiparallel supramolecular beta-sheet from a synthetic tripeptide: a crystallographic signature

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Banerjee, A. , Maji, S.K., Drew, M.G.B. , Haldar, D. and Banerjee, A. (2003) An amyloid-like fibril forming antiparallel supramolecular beta-sheet from a synthetic tripeptide: a crystallographic signature. Tetrahedron Letters, 44 (35). pp. 6741-6744. ISSN 0040-4039

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To link to this item DOI: 10.1016/S0040-4039(03)01642-3

Abstract/Summary

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 beta-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. (C) 2003 Elsevier Ltd. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:10987
Uncontrolled Keywords:Aib, antiparallel beta-sheet, amyloid-like fibrils, self-assembly , SOLID-STATE NMR, STRUCTURAL CHARACTERIZATION, PROTEIN FIBRILLOGENESIS, PARKINSONS-DISEASE, ALZHEIMERS-DISEASE, ALPHA-SYNUCLEIN, LEWY BODIES, PEPTIDE, AGGREGATION, INCLUSIONS
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