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Expanding the Loop Segments in β-hairpin Nonapeptides in Protein Folding and Biological Functions

Rajagopal Appavu*
Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, Texas, United States Minor Outlying Islands
*Corresponding Author : Rajagopal Appavu
Experimental Radiation Oncology
The University of Texas MD Anderson Cancer Center
1515 Holcombe Blvd, Y6.6006 Houston
Texas 77030, United States Minor Outlying Islands
Tel: 409-256-9987
Fax: 713-794-5369
E-mail: [email protected]
Received January 28, 2016; Accepted February 18, 2016; Published February 23, 2016
Citation: Appavu R (2016) Expanding the Loop Segments in β-hairpin Nonapeptides in Protein Folding and Biological Functions. Transcriptomics 4:e116. doi:10.4172/2329-8936.1000e116
Copyright: © 2016 Appavu R. 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.

 

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Abstract

Analysis of β-hairpins in proteins, have revealed several examples of antiparallel β-strands connected by short linking segments, which contain more than two residues.The design of synthetic peptide hairpins formed with central two residue turns has been facilitated by the ease with which specific types of β-turn structures can be generated in short peptides. Earlier work in this laboratory has addressed the question of expanding the central connecting loop in designed peptide β-hairpins.

Editorial
Analysis of β-hairpins in proteins, have revealed several examples of antiparallel β-strands connected by short linking segments, which contain more than two residues [1-6].The design of synthetic peptide hairpins formed with central two residue turns has been facilitated by the ease with which specific types of β-turn structures can be generated in short peptides. Earlier work in this laboratory has addressed the question of expanding the central connecting loop in designed peptide β-hairpins. (Figure 1) schematically compares the two residue and three residue β-hairpins. Successful expansion of the loop region has been achieved using a centrally positioned DPro-LPro-DAla segment. A detailed NMR study of the nonapeptide Boc-Leu-Phe-Val-DPro-LPro- DAla-Leu-Phe-Val-OMe revealed that registered antiparallel strands are formed in solution. The hairpin facilitating three residue turn requires the DAla residue to adopt an αL conformation (φ ∼60°, ψ ∼30°) [2-7]. When the residue at position (6) was replaced by LAla, the nonapeptide yielded a two residue hairpin structure with the DPro-LPro segment forming a type-II′ β-turn. The LAla(6) residue is now incorporated into the C-terminus segment, with “slipped” strand registry. The significant conformational transitions were appeared replacing the DAla(6) to Gly(6), and LAla(6) in the protein secondary structure conformation. This conformation, referred to as a “slipped hairpin” structure, together with the three residue hairpin is illustrated in Figure 1. Inspection of the structures shown in Figure 1 suggests the two conformations are clearly distinguishable, if the aromatic ring orientations are considered. Thus, in addition to cross-strand nuclear over hauser effects (NOEs) and delineation of NH bonded groups, aromatic proton chemical shifts may prove to be a convenient diagnostic for the conformations present in this class of designed nonapeptides. The Editorial describes a systematic analysis of peptides in which the residue at position 6 is varied in the sequence Boc-Leu-Phe-Val-DPro-LPro-Yyy-Leu-Phe-Val- OMe. Studies on related peptides in which LPro(5) is substituted by Aib and LAla are also reported in this laboratory [5-7]. NOE effect clearly reveals the replacement of Xxx and Yyy positions L, and D Amino Acids yield a mixed population of three residue β-hairpins and two residue β-hairpins stabilization of Aromatic-Aromatic interactions.
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