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Design of supramolecular beta-sheet forming beta-turns containing aromatic rings and non-coded alpha-aminoisobutyric acid and the formation of flat fibrillar structures through self-assembly

Kar, S., Dutta, A., Drew, M.G.B., Koley, P. and Pramanik, A. (2009) Design of supramolecular beta-sheet forming beta-turns containing aromatic rings and non-coded alpha-aminoisobutyric acid and the formation of flat fibrillar structures through self-assembly. Supramolecular Chemistry, 21 (8). pp. 681-690. ISSN 1061-0278

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To link to this item DOI: 10.1080/10610270802709378

Abstract/Summary

Single crystal X-ray diffraction studies show that the three designed tripeptides Boc-Leu-Aib-m-NA-NO2 (I), Boc-Phe-Aib-m-NA-NO2 (II) and Boc-Pro-Aib-m-ABA-OMe (III) (Aib, -aminoisobutyric acid; m-NA, m-nitroaniline; m-ABA, m-aminobenzoic acid; Boc, t-butyloxycarbonyl) containing aromatic rings in the backbones adopt -turn structures that are self-assembled through intermolecular hydrogen bonds and van der Waals interactions to create layers of -sheets. Solvent-dependent NMR titration and CD studies show that the -turn structures of the peptides also exist in the solution phase. The field emission scanning electron microscopic and transmission electron microscopic images of the peptides in the solid state reveal fibrillar structures of flat morphology that are formed through -sheet mediated self-assembly of the preorganised -turn building blocks.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11386
Uncontrolled Keywords:peptide, -aminoisobutyric acid, -turn, -sheets, flat morphology, 1ST CRYSTALLOGRAPHIC SIGNATURE, PEPTIDE-AMPHIPHILE NANOFIBERS, AMYLOID-LIKE FIBRILS, X-RAY-DIFFRACTION, SOLID-STATE, AMINO-ACIDS, SOLUTION CONFORMATIONS, SYNTHETIC TRIPEPTIDE, CORNER RESIDUES, PARALLEL

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