Владимир Егоров » Публикация
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Опубликовано
2013-12-24
Опубликовано на SciPeople2013-12-24 23:06:57
ЖурналInternational Journal of Peptides
Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein
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
Аннотация
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.