Overlapping Double Turn Conformations Adopted by Tetrapeptides Containing Non-Coded α-Amino Isobutyric Acid (AIB) and Formation of Tape-Like Structures Through Supramolecular Helix Mediated Self-Assembly

Author(s): Sudeshna Kar, Arpita Dutta, M. G.B. Drew, Pradyot Koley, Animesh Pramanik

Journal Name: Protein & Peptide Letters

Volume 16 , Issue 9 , 2009


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Abstract:

Single crystal X-ray diffraction studies and solvent dependent 1H 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.

Keywords: Peptide, α-Aminoisobutyric acid, Double turn, Self-assembly, Supramolecular helix, Tape-like structures

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Article Details

VOLUME: 16
ISSUE: 9
Year: 2009
Page: [1063 - 1073]
Pages: 11
DOI: 10.2174/092986609789055386
Price: $65

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