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Supramolecular peptide helix from a novel double turn forming peptide containing a beta-amino acid

Banerjee, 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

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To link to this item DOI: 10.1016/S0040-4039(02)02675-8

Abstract/Summary

A 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.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:10986
Uncontrolled Keywords:supramolecular helix, Aib, beta-Ala, fibrils , MOLECULAR RECOGNITION, ELECTRON-MICROSCOPY, FIBRIL FORMATION, WATER-MOLECULES, AMYLOID FIBRIL, ALPHA-HELIX, MOTIFS, NUCLEATION, CHEMISTRY, HELICATE

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