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
- International Journal of Peptides , 2013
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 b...
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.
Vladimir V. Egorov, Oleg V. Matusevich, Aram A. Shaldzhyan, et al., “Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein,” International Journal of Peptides, vol. 2013, Article ID 370832, 5 pages, 2013. doi:10.1155/2013/370832