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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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 |
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Publication: | CHEMISTRY-A EUROPEAN JOURNAL |
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) |
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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