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Understanding the conformational analysis of gababutin based hybrid peptides

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Abstract

Constrained γ-amino acid gababutin (Gbn) based peptides that form different conformations have been synthesized. Striving to rationalize the impact of side chain orientations framing tetrapeptide-based supramolecular organic frameworks and morphological entities, Gbn incorporated hybrid peptides Boc-Gbn-Aib-Aaa-Aib-OMe (where Aaa = Phe(F) for peptide 1, Leu(L) for peptide 2 and Tyr(Y) for peptide 3) were synthesized by changing the amino acid at the third position. The solution state dual folded conformation (C12/C10 H-bonded) is probed by 2D NMR spectroscopy in support of a DMSO-d6 titration and VT NMR experiments. Peptides 1–3 adopt a C12/C10 type H-bonded dual folded conformation in the crystal state. In addition, distinct supramolecular frameworks result from the modification and orientation of the third residue side chain of peptides 1–3. A solvent induced morphological diversity of peptides 1–3 is attained by modifying the side chain backbone of the tetrapeptides, which are investigated by various microscopic (SEM and AFM) studies. Gbn-based peptides 1–3 show significant morphological and supramolecular packing properties, which are fairly different from those of their gabapentin (Gpn) based analogue peptides.

Graphical abstract: Understanding the conformational analysis of gababutin based hybrid peptides

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Publication details

The article was received on 05 Jan 2018, accepted on 06 Feb 2018 and first published on 06 Feb 2018


Article type: Paper
DOI: 10.1039/C8OB00035B
Citation: Org. Biomol. Chem., 2018, Advance Article
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    Understanding the conformational analysis of gababutin based hybrid peptides

    M. Konda, R. G. Jadhav, S. Maiti, S. M. Mobin, B. Kauffmann and A. K. Das, Org. Biomol. Chem., 2018, Advance Article , DOI: 10.1039/C8OB00035B

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