Supramolecular peptide helix from a novel double turn forming peptide containing a beta-amino acidBanerjee, A. , Maji, S.K., Drew, M.G.B., Haldar, D. and Banerjee, A. (2003) Supramolecular peptide helix from a novel double turn forming peptide containing a beta-amino acid. Tetrahedron Letters, 44 (4). pp. 699-702. ISSN 0040-4039 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/S0040-4039(02)02675-8 Abstract/SummaryA single-crystal X-ray diffraction study of the terminally protected tetrapeptide Boc-beta-Ala-Aib-Leu-Aib-OMe 1 (Aib: alpha-aminoisobutyric acid; beta-Ala: beta-Alanine) reveals that it adopts a new type of double turn structure which self-associates to form a unique supramolecular helix through intermolecular hydrogen bonds. Scanning electron microscopic studies show that peptide 1 exhibits amyloid-like fibrillar morphology in the solid state. (C) 2003 Elsevier Science Ltd. All rights reserved.
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