Self-assembly of beta-turn forming synthetic tripeptides into supramolecular beta-sheets and amyloid-like fibrils in the solid stateMaji, 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 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1016/j.tet.2004.02.019 Abstract/SummaryWe 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.
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