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

Banerjee, Arijit ; Maji, Samir Kumar ; Drew, Michael G. B. ; Haldar, Debasish ; Banerjee, Arindam (2003) Supramolecular peptide helix from a novel double turn forming peptide containing a β-amino acid Tetrahedron Letters, 44 (4). pp. 699-702. ISSN 0040-4039

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/S0040-4039(02)02675-8

Abstract

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.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Supramolecular Helix; Aib; β-Ala; Fibrils
ID Code:99504
Deposited On:07 Nov 2016 11:18
Last Modified:12 Feb 2018 12:21

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