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Formation of fibrillar structures through self-assembly of designed peptide turns

Kar, S., Drew, M.G.B. and Pramanik, A. (2009) Formation of fibrillar structures through self-assembly of designed peptide turns. Arkivoc (12). pp. 43-59. ISSN 1551-7004

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Official URL: http://www.arkat-usa.org/

Abstract/Summary

Three tripeptides Boc-Phe-Aib-Val-OMe (1), Boc-Leu-Aib-p-NA-NO2 (2) and Boc-Pro-Aib-m-NA-NO2 (3) (Aib: alpha-aminoisobutyric acid; p- and m-NA: para- and meta-nitroaniline) have been designed by incorporating aromatic rings to study the self-assembly and fibril formation. Single crystal X-ray diffraction studies show that all the peptides adopt turn-like structures that are self-assembled through intermolecular hydrogen bonds and van der Waals interactions to create layers of beta-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 (FE-SEM) images of the peptides in the solid state reveal fibrillar structures of flat morphology that are formed through beta-sheet mediated self-assembly of the preorganized turn building blocks.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11384
Uncontrolled Keywords:Peptides, turns, self-assembly, beta-sheet, fibrils, 1ST CRYSTALLOGRAPHIC SIGNATURE, SUPRAMOLECULAR BETA-SHEETS, AMYLOID-LIKE FIBRILS, CODED AMINO-ACIDS, X-RAY-DIFFRACTION, SOLID-STATE, SOLUTION CONFORMATIONS, AMPHIPHILE NANOFIBERS, SYNTHETIC, TRIPEPTIDE, CORNER RESIDUES

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