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Amyloid-like fibril-forming supramolecular beta-sheets from a beta-turn forming tripeptide containing non-coded amino acids: the crystallographic signature

Banerjee, A., Maji, S.K., Drew, M.G.B., Haldar, D. and Banerjee, A. (2003) Amyloid-like fibril-forming supramolecular beta-sheets from a beta-turn forming tripeptide containing non-coded amino acids: the crystallographic signature. Tetrahedron Letters, 44 (2). pp. 335-339. ISSN 0040-4039

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To link to this item DOI: 10.1016/S0040-4039(02)02570-4

Abstract/Summary

The crystal structure of a terminally protected tripeptide Boc-Leu-Aib-beta-Ala-OMe 1 containing non-coded amino acids reveals that it adopts a beta-turn structure, which sell-assembles to form a supramolecular beta-sheet via non-covalent interactions. The SEM image of peptide 1 exhibits amyloid-like fibrillar morphology in the solid state. (C) 2002 Elsevier Science Ltd. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:10985
Uncontrolled Keywords:beta-turn, Aib, beta-Ala, beta-sheet, amyloid fibrils , X-RAY-DIFFRACTION, ALTERNATIVE CONFORMATIONS, PROTEIN FIBRILLOGENESIS, ALZHEIMERS-DISEASE, MICROSCOPY, PEPTIDES, PARALLEL, MODEL

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