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

Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png International Journal of Peptides Hindawi Publishing Corporation

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Publisher
Hindawi Publishing Corporation
Copyright
Copyright © 2013 Vladimir V. Egorov et al.
ISSN
1687-9767
eISSN
1687-9775
Publisher site
See Article on Publisher Site

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.

Journal

International Journal of PeptidesHindawi Publishing Corporation

Published: Dec 24, 2013

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