Chinnasamy Selvakkumar1*, Eashwarwark Vikram Reddy2, Kesavanarayanan Krishnan Selvarajan3, Nazeerullah Rahamuthullah1 and Muftha Mohamed Zarmouh1
1Department of Microbiology and Immunology, Faculty of Medicine, Misurata University, Libya
2Department of Microbiology, Sri Lakshmi Narayana Institute of Medical Sciences, Bharath University, Puducherry, India
3Department of Pharmacology, SRM College of Pharmacy, SRM University, Chennai, India
Received: 03 March, 2016; Accepted: 26 April, 2016; Published: 04 May, 2016
Dr. Chinnasamy Selvakkumar, Department of Microbiology and Immunology, Faculty of Medicine, Misurata University, Libya, E-mail:
Selvakkumar C, Reddy EV, Selvarajan KK, Rahamuthullah N, Zarmouh MM (2016) Design of Peptide Models for β-Hairpins and Equilibrating Helix-Hairpin Structures. Int J Nanomater Nanotechnol Nanomed 2(1): 015-017. DOI: 10.17352/2455-3492.000009
© 2016 Selvakkumar C, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
It is well established that synthetic peptides containing a centrally positioned Type-I or Type-II β-turn can form well folded peptide hairpins (1). Earlier studies from this laboratory have established that D-Pro-Xxx segments nucleate β-hairpin structures, with formation of a central Type-II β-turn (2). The octapeptide (Boc-Leu-Phe-Val-Aib-D-Ala-Leu-Phe- Val-OMe) is a rare example of a synthetic peptide hairpin, containing a central Type-I β-turn. Hairpins with Type-I turns are considerably more twisted than their Type-II counterparts. The Aib-Xxx segment has also been shown to adopt a Type-I β-turn structure, resulting in incorporation into the centre of a long synthetic, helical peptide (3) (Figures 1,2).