Table of Contents
International Journal of Peptides
Volume 2013 (2013), Article ID 370832, 5 pages
Research Article

Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein

1Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia
2Department of Molecular and Radiation Biophysics, Kurchatov Institute, FSBI St. Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina 188300, Russia
3Faculty of Chemistry, Saint Petersburg State University, Saint Petersburg 198504, Russia

Received 3 October 2013; Revised 3 December 2013; Accepted 9 December 2013

Academic Editor: Tzi Bun Ng

Copyright © 2013 Vladimir V. Egorov et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


A mirror-symmetry motif was discovered in the N-terminus of the influenza virus PB1 protein. Structure of peptide comprised of the corresponding part of PB1 (amino acid residues 6-25) was investigated by circular dichroism and in silico modeling. We found that peptide PB1 (6-25) in solution assumes beta-hairpin conformation. A truncated peptide PB1 (6-13), containing only half of the mirror-symmetry motif, appeared to stabilize the beta-structure of the original peptide and, at high concentrations, was capable of reacting with peptide to form insoluble aggregates in vitro. Ability of PB1 (6-13) peptide to interact with the N-terminal domain of PB1 protein makes it a potential antiviral agent that inhibits PA-PB1 complex formation by affecting PB1 N-terminus structure.