tetano
Editor, Senior Moderator
Int J Pept. 2013;2013:370832. doi: 10.1155/2013/370832. Epub 2013 Dec 24.
Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein.
Egorov VV1, Matusevich OV2, Shaldzhyan AA3, Skvortsov AN3, Zabrodskaya YA3, Garmay YP1, Landa SB4, Lebedev DV4, Zarubayev VV3, Sirotkin AK3, Vasin AV3, Kiselev OI3.
Author information
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.
PMID:
24454411
[PubMed]
Free full text
http://www.ncbi.nlm.nih.gov/pubmed/24454411
Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein.
Egorov VV1, Matusevich OV2, Shaldzhyan AA3, Skvortsov AN3, Zabrodskaya YA3, Garmay YP1, Landa SB4, Lebedev DV4, Zarubayev VV3, Sirotkin AK3, Vasin AV3, Kiselev OI3.
Author information
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.
PMID:
24454411
[PubMed]
Free full text
http://www.ncbi.nlm.nih.gov/pubmed/24454411