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C-11/C-9 Helical Folding in alpha beta Hybrid Peptides Containing 1-Amino-cyclohexane acetic acid (beta(3,3)-Ac(6)c)

Wani, Naiem Ahmad and Raghothama, Srinivasarao and Singh, Umesh Prasad and Rai, Rajkishor (2017) C-11/C-9 Helical Folding in alpha beta Hybrid Peptides Containing 1-Amino-cyclohexane acetic acid (beta(3,3)-Ac(6)c). In: CHEMISTRY-A EUROPEAN JOURNAL, 23 (35). pp. 8364-8370.

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Official URL: http://dx.doi.org/10.1002/chem.201700265

Abstract

The present study describes the solid-state conformation of ab hybrid peptides, Boc-Leu-beta(3,3)-Ac(6)c-OH, P1; Boc-Leu-beta(3,3)-Ac(6)c-Leu-beta(3,3)-Ac(6)c-OMe, P2; and Boc-Leu-beta(3,3)-Ac(6)c-Leu-beta(3,3)-Ac(6)c-Leu-OMe, P3. The dipeptide P1 adopts extended conformations, whereas tetrapeptide P2 and pentapeptide P3 favor a helical conformation stabilized by mixed types of C-11/C-9 intramolecular hydrogen bonds. In peptide P3, the amino group of beta(3,3)-Ac(6)c(2) and beta(3,3)-Ac(6)c(4) residues occupies axial orientation, whereas in P2 it occupies axial and equatorial orientations for residues beta(3,3)-Ac(6)c(2) and beta(3,3)-Ac(6)c(4), respectively. The self-assembly of P3 forms channels filled with solvent molecules that present interesting patterns.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the WILEY-V C H VERLAG GMBH, POSTFACH 101161, 69451 WEINHEIM, GERMANY
Department/Centre: Division of Chemical Sciences > NMR Research Centre (Formerly Sophisticated Instruments Facility)
Depositing User: Id for Latest eprints
Date Deposited: 14 Jul 2017 05:06
Last Modified: 14 Jul 2017 05:06
URI: http://eprints.iisc.ac.in/id/eprint/57376

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