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Saint Petersburg, Russia

Egorov V.V.,RAS Petersburg Nuclear Physics Institute | Lebedev D.V.,RAS Petersburg Nuclear Physics Institute | Shaldzhyan A.A.,FSBI Research Institute of Influenza | Sirotkin A.K.,FSBI Research Institute of Influenza | And 5 more authors.
Prion | Year: 2014

The fibrillogenesis of a peptide corresponding to residues 35-51 of human α-lactalbumin (1GYDTQAIVENNESTEYG17) can be dramatically enhanced by the addition of a tetrapeptide TDYG homologous to its C-terminus (TEYG). Generation of spontaneous hydrolytic products similar to this peptide was demonstrated by mass-spectrometry analysis of GYDTQAIVE NNESTEYG peptide solution components during fibrillogenesis. Possible mechanisms and roles of short peptides in protein metabolism are discussed. © 2014 Taylor & Francis Group, LLC. Source


Egorov V.V.,RAS Petersburg Nuclear Physics Institute | Matusevich O.V.,Saint Petersburg State University | Shaldzhyan A.A.,FSBI Research Institute of Influenza | Skvortsov A.N.,FSBI Research Institute of Influenza | And 8 more authors.
International Journal of Peptides | Year: 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 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. © 2013 Vladimir V. Egorov et al. Source

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