This research article describes the design of peptide models to form beta-hairpin and helix-hairpin structures. The researchers established that peptides containing a centrally positioned Type-I or Type-II beta-turn can form well-folded beta-hairpin structures. Earlier studies from their laboratory showed that D-Pro-Xxx segments nucleate beta-hairpin structures through the formation of a central Type-II beta-turn. The article provides information on designing peptide models to achieve different secondary structures like beta-hairpins and helix-hairpin structures.

1. International Journal of
Nanomaterials,
Nanotechnology and
Nanomedicine – ISSN: 2455-3492
Peertechz Journals

2. Research Article
Design of Peptide Models for β-Hairpins
and Equilibrating Helix-Hairpin
Structures
 Chinnasamy Selvakkumar*, Eashwarwark Vikram Reddy, Kesavanarayanan
Krishnan Selvarajan, Nazeerullah Rahamuthullah and Muftha Mohamed
Zarmouh
 *Corresponding author: Dr. Chinnasamy Selvakkumar, Department of
Microbiology and Immunology, Faculty of Medicine, Misurata University,
Libya,
 Dates: Received: 03 March, 2016; Accepted: 26 April, 2016; Published: 04
May, 2016
 Citation: 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.

3. Introduction
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).

4. Thank you
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