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Issue 7, 2017
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Synthetic minimalistic tryptophan zippers as a chiroptical switch

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Abstract

In this paper, we presented a new design strategy for a peptide-based chiral supramolecular assembly. A series of aryl linked peptides 1a–1f were designed and synthesized. The bis-urea peptides 1a–1c self-assembled into a helical supramolecular arrangement resembling Trp zipper (Trpzip) structures present in proteins. Interestingly, a dihydrogenphosphate anion, upon binding to the assembly, could invert the chirality of the supramolecular assembly which could be reverted to the original by the addition of water. This chiroptical behavior can be repeated several times. Microscopy analysis showed that the supramolecular helices were assembled to form spheres. In addition to that, we also found that the handedness of supramolecular chirality is dependent on the position of Trp residues on the aromatic scaffold. Both left and right handed helical supramolecular arrangements were obtained by placing L-Trp residues at different positions on the aromatic core. The unprecedented Trpzip in these designed small peptidomimetics will stimulate more work in the area of peptide-based assemblies.

Graphical abstract: Synthetic minimalistic tryptophan zippers as a chiroptical switch

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Publication details

The article was received on 30 Nov 2016, accepted on 18 Jan 2017 and first published on 18 Jan 2017


Article type: Paper
DOI: 10.1039/C6OB02617F
Citation: Org. Biomol. Chem., 2017,15, 1661-1669
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    Synthetic minimalistic tryptophan zippers as a chiroptical switch

    V. Haridas, S. Sadanandan, S. Dhawan, R. Mishra, I. Jain, G. Goel, Y. Hu and S. Patel, Org. Biomol. Chem., 2017, 15, 1661
    DOI: 10.1039/C6OB02617F

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