Issue 5, 2015

The role of N-terminal proline in stabilizing the Ant–Pro zipper motif

Abstract

Hetero-chiral hybrid peptides of the general sequence LαβnDαβn featuring proline (Pro, a constrained α-amino acid) and anthranilic acid (Ant, a constrained β-amino acid) as building blocks, where n = 2, 4 etc., form a three-dimensional zipper-like architecture. These zipper peptides attain stable conformation by balancing the co-operative contribution of two competing non-covalent forces, namely hydrogen bonding and aromatic stacking. However, the selection of the N-terminal residue also stands to be one of the key contributors in stabilising the unusually long-range intramolecular hydrogen bond, featuring 26 atoms in the H-bonded ring observed at the termini. This article deals with the substitution alterations at the N-terminus of the zipper motif and their consequent influences on its structure and stability. In this study, the N-terminal Pro residue of the zipper motif was substituted with a flexible amino acid, alanine, and a constrained acyclic amino acid, 2-aminoisobutyric acid, to investigate the role of N-terminal proline in stabilizing the Ant–Pro zipper motif, and its stabilities were assessed by employing solution-state NMR and restrained MD simulation studies.

Graphical abstract: The role of N-terminal proline in stabilizing the Ant–Pro zipper motif

Supplementary files

Article information

Article type
Paper
Submitted
26 Nov 2014
Accepted
08 Mar 2015
First published
09 Mar 2015

New J. Chem., 2015,39, 3327-3332

Author version available

The role of N-terminal proline in stabilizing the Ant–Pro zipper motif

S. Kheria, R. V. Nair, A. S. Kotmale, P. R. Rajamohanan and G. J. Sanjayan, New J. Chem., 2015, 39, 3327 DOI: 10.1039/C4NJ02151G

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements