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Overlapping double turn conformations adopted by tetrapeptides containing non-coded alpha-Amino Isobutyric Acid (AIB) and formation of tape-like structures through supramolecular helix mediated self-assembly

Kar, S., Dutta, A., Drew, M. G. B., Koley, P. and Pramanik, A. (2009) Overlapping double turn conformations adopted by tetrapeptides containing non-coded alpha-Amino Isobutyric Acid (AIB) and formation of tape-like structures through supramolecular helix mediated self-assembly. Protein and Peptide Letters, 16 (9). pp. 1063-1073. ISSN 0929-8665

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To link to this item DOI: 10.2174/092986609789055386

Abstract/Summary

Single crystal X-ray diffraction studies and solvent dependent H-1 NMR titrations reveal that a set of four tetrapeptides with general formula Boc-Xx(1)-Aib(2)-Yy(3)-Zz(4)-OMe, where Xx, Yy and Zz are coded L- amino acids, adopt equivalent conformations that can be described as overlapping double turn conformations stabilized by two 4 -> 1 intramolecular hydrogen bonds between Yy(3)-NH and Boc C=O and Zz(4)-NH and Xx(1)C=O. In the crystalline state, the double turn structures are packed in head-to-tail fashion through intermolecular hydrogen bonds to create supramolecular helical structures. Field emission scanning electron microscopic (FE-SEM) images of the tetrapeptides in the solid state reveal that they can form flat tape-like structures. The results establish that synthetic Aib containing supramolecular helices can form highly ordered self-aggregated amyloid plaque like human amylin.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11385
Uncontrolled Keywords:Peptide, alpha-Aminoisobutyric acid, Double turn, Self-assembly, Supramolecular helix, Tape-like structures, 1ST CRYSTALLOGRAPHIC SIGNATURE, AMYLOID FIBRIL FORMATION, BETA-SHEET, PEPTIDE, SOLID-STATE, HUMAN CALCITONIN, CORNER RESIDUES, TRIPEPTIDE, PENTAPEPTIDE, TEMPLATES, NANOWIRES

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