{"_id":"LM4akRE4RDTuwWuM5","bibbaseid":"anonymous-theamyloidogenicityoftheinfluenzaviruspb1derivedpeptideshedslightonitsantiviralactivity-2018","bibdata":{"bibtype":"article","type":"article","author":[{"propositions":[],"lastnames":["Zabrodskaya"],"firstnames":["Y.A."],"suffixes":[]},{"propositions":[],"lastnames":["Lebedev"],"firstnames":["D.V."],"suffixes":[]},{"propositions":[],"lastnames":["Egorova"],"firstnames":["M.A."],"suffixes":[]},{"propositions":[],"lastnames":["Shaldzhyan"],"firstnames":["A.A."],"suffixes":[]},{"propositions":[],"lastnames":["Shvetsov"],"firstnames":["A.V."],"suffixes":[]},{"propositions":[],"lastnames":["Kuklin"],"firstnames":["A.I."],"suffixes":[]},{"propositions":[],"lastnames":["Vinogradova"],"firstnames":["D.S."],"suffixes":[]},{"propositions":[],"lastnames":["Klopov"],"firstnames":["N.V."],"suffixes":[]},{"propositions":[],"lastnames":["Matusevich"],"firstnames":["O.V."],"suffixes":[]},{"propositions":[],"lastnames":["Cheremnykh"],"firstnames":["T.A."],"suffixes":[]},{"propositions":[],"lastnames":["Dattani"],"firstnames":["R."],"suffixes":[]},{"propositions":[],"lastnames":["Egorov"],"firstnames":["V.V."],"suffixes":[]}],"title":"The amyloidogenicity of the influenza virus PB1-derived peptide sheds light on its antiviral activity","journal":"Biophysical Chemistry","year":"2018","volume":"234","pages":"16-23","doi":"10.1016/j.bpc.2018.01.001","note":"cited By 3","url":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-85040105182&doi=10.1016%2fj.bpc.2018.01.001&partnerID=40&md5=a3bb20ebdf653535639a94e2153decc0","affiliation":"Research Institute of Influenza, Ministry of Healthcare of the Russian Federation, St. Petersburg, Russian Federation; Petersburg Nuclear Physics Institute named by B. P. Konstantinov of National Research Center “Kurchatov Institute”, Gatchina, Russian Federation; Peter the Great SaintPetersburg State Polytechnic University, St. Petersburg, Russian Federation; Joint Institute for Nuclear Research, Dubna, Russian Federation; Moscow Institute of Physics and Technology (State University), Moscow, Russian Federation; NanoTemper Technologies Rus, St. Petersburg, Russian Federation; European Synchrotron Radiation Facility, Grenoble, France; Federal State Budgetary Scientific Institution “Institute of Experimental Medicine”, St. Petersburg, Russian Federation","abstract":"The influenza virus polymerase complex is a promising target for new antiviral drug development. It is known that, within the influenza virus polymerase complex, the PB1 subunit region from the 1st to the 25th amino acid residues has to be is in an alpha-helical conformation for proper interaction with the PA subunit. We have previously shown that PB1(6–13) peptide at low concentrations is able to interact with the PB1 subunit N-terminal region in a peptide model which shows aggregate formation and antiviral activity in cell cultures. In this paper, it was shown that PB1(6–13) peptide is prone to form the amyloid-like fibrillar aggregates. The peptide homo-oligomerization kinetics were examined, and the affinity and characteristic interaction time of PB1(6–13) peptide monomers and the influenza virus polymerase complex PB1 subunit N-terminal region were evaluated by the SPR and TR-SAXS methods. Based on the data obtained, a hypothesis about the PB1(6–13) peptide mechanism of action was proposed: the peptide in its monomeric form is capable of altering the conformation of the PB1 subunit N-terminal region, causing a change from an alpha helix to a beta structure. This conformational change disrupts PB1 and PA subunit interaction and, by that mechanism, the peptide displays antiviral activity. © 2018 Elsevier B.V.","author_keywords":"Amyloid-like fibrils; Antiviral peptides; Conformational transition; Influenza A virus polymerase complex; PB1 subunit","funding_details":"N08.11.0080, 14.","key":"Zabrodskaya201816","id":"Zabrodskaya201816","bibbaseid":"anonymous-theamyloidogenicityoftheinfluenzaviruspb1derivedpeptideshedslightonitsantiviralactivity-2018","role":"author","urls":{"Paper":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-85040105182&doi=10.1016%2fj.bpc.2018.01.001&partnerID=40&md5=a3bb20ebdf653535639a94e2153decc0"},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bio.pnpi.nrcki.ru/wp-content/uploads/2019/12/lbm_2019_10.txt","dataSources":["YYLjupmCazkNqWNEJ"],"keywords":[],"search_terms":["amyloidogenicity","influenza","virus","pb1","derived","peptide","sheds","light","antiviral","activity"],"title":"The amyloidogenicity of the influenza virus PB1-derived peptide sheds light on its antiviral activity","year":2018}