In:
International Journal of Peptides, Hindawi Limited, Vol. 2013 ( 2013-12-24), p. 1-5
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.
Type of Medium:
Online Resource
ISSN:
1687-9767
,
1687-9775
Language:
English
Publisher:
Hindawi Limited
Publication Date:
2013
detail.hit.zdb_id:
2570929-X