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

Title: 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

Volume: 16 Issue: 9

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

Affiliation:

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

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.

Cite this article as:

Kar Sudeshna, Dutta Arpita, Drew G.B. M., Koley Pradyot and Pramanik Animesh, 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, Protein & Peptide Letters 2009; 16 (9) . https://dx.doi.org/10.2174/092986609789055386