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

Vladimir V Egorov; Oleg V Matusevich; Aram A Shaldzhyan; Alexey N Skvortsov; Yana A Zabrodskaya; Yuri P Garmay; Sergey B Landa; Dmitry V Lebedev; Vladimir V Zarubayev; Alexey K Sirotkin; Andrey V Vasin; Oleg I Kiselev

doi:10.1155/2013/370832

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

Int J Pept. 2013:2013:370832. doi: 10.1155/2013/370832. Epub 2013 Dec 24.

Affiliations

¹ Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia ; Department of Molecular and Radiation Biophysics, Kurchatov Institute, FSBI St. Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina 188300, Russia.
² Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia ; Faculty of Chemistry, Saint Petersburg State University, Saint Petersburg 198504, Russia.
³ Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia.
⁴ Department of Molecular and Radiation Biophysics, Kurchatov Institute, FSBI St. Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina 188300, Russia.

Abstract

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.