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Self-assembly of beta-turn forming synthetic tripeptides into supramolecular beta-sheets and amyloid-like fibrils in the solid state

Maji, S.K., Haldar, D. , Drew, M.G.B., Banerjee, A. , Das, A.K. and Banerjee, A. (2004) Self-assembly of beta-turn forming synthetic tripeptides into supramolecular beta-sheets and amyloid-like fibrils in the solid state. Tetrahedron, 60 (14). pp. 3251-3259. ISSN 0040-4020

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To link to this item DOI: 10.1016/j.tet.2004.02.019

Abstract/Summary

We have described here the self-assembling properties of the synthetic tripeptides Boc-Ala(1)-Aib(2) -Val (3)-OMe 1, BocAla(l)-Aib(2)-Ile(3)-OMe 2 and Boc-Ala(l)-Gly(2)-Val(3)-OMe 3 (Aib=alpha-arnino isobutyric acid, beta-Ala=beta-alanine) which have distorted beta-turn conformations in their respective crystals. These turn-forming tripeptides self-assemble to form supramolecular beta-sheet structures through intermolecular hydrogen bonding and other noncovalent interactions. The scanning electron micrographs of these peptides revealed that these compounds form amyloid-like fibrils, the causative factor for many neurodegenerative diseases including Alzheimer's disease, Huntington's disease and Prion-related encephalopathies. (C) 2004 Elsevier 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:11454
Uncontrolled Keywords:amyloid-like fibril, beta-turn, supramolecular beta-sheet, self-assembling peptides , CRYSTALLOGRAPHIC SIGNATURE, ALZHEIMERS-DISEASE, PEPTIDE NANOTUBES, PROTEIN FIBRILLOGENESIS, ORGANIC NANOTUBES, AGGREGATION, CHANNEL

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