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dc.contributor.authorGerszon, Joanna
dc.contributor.authorRodacka, Aleksandra
dc.contributor.authorSerafin, Eligiusz
dc.contributor.authorBuczkowski, Adam
dc.contributor.authorMichlewska, Sylwia
dc.contributor.authorBielnicki, Antoni
dc.contributor.editorPermyakov, Eugene A.
dc.identifier.citationGerszon J, Serafin E, Buczkowski A, Michlewska S, Bielnicki JA, Rodacka A (2018) Functional consequences of piceatannol binding to glyceraldehyde-3-phosphate dehydrogenase. PLoS ONE 13(1): e0190656. journal.pone.0190656pl_PL
dc.description.abstractGlyceraldehyde-3-phosphate dehydrogenase (GAPDH) is one of the key redox-sensitive proteins whose activity is largely affected by oxidative modifications at its highly reactive cysteine residue in the enzyme’s active site (Cys149). Prolonged exposure to oxidative stress may cause, inter alia, the formation of intermolecular disulfide bonds leading to accumulation of GAPDH aggregates and ultimately to cell death. Recently these anomalies have been linked with the pathogenesis of Alzheimer’s disease. Novel evidences indicate that low molecular compounds may be effective inhibitors potentially preventing the GAPDH translocation to the nucleus, and inhibiting or slowing down its aggregation and oligomerization. Therefore, we decided to establish the ability of naturally occurring compound, piceatannol, to interact with GAPDH and to reveal its effect on functional properties and selected parameters of the dehydrogenase structure. The obtained data revealed that piceatannol binds to GAPDH. The ITC analysis indicated that one molecule of the tetrameric enzyme may bind up to 8 molecules of polyphenol (7.3 ± 0.9). Potential binding sites of piceatannol to the GAPDH molecule were analyzed using the Ligand Fit algorithm. Conducted analysis detected 11 ligand binding positions. We indicated that piceatannol decreases GAPDH activity. Detailed analysis allowed us to presume that this effect is due to piceatannol ability to assemble a covalent binding with nucleophilic cysteine residue (Cys149) which is directly involved in the catalytic reaction. Consequently, our studies strongly indicate that piceatannol would be an exceptional inhibitor thanks to its ability to break the aforementioned pathologic disulfide linkage, and therefore to inhibit GAPDH aggregation. We demonstrated that by binding with GAPDH piceatannol blocks cysteine residue and counteracts its oxidative modifications, that induce oligomerization and GAPDH aggregation.pl_PL
dc.description.sponsorshipThis work is supported by a grant from the Faculty of Biology and Environmental Protection, University of Lodz (grant number: B1711000001504.02) and by National Science Centre, Poland (grant number 2017/25/N/NZ1/02849) and supported by subsidy for young scientists (Faculty of Biology and Environmental Protection, University of Lodz). Bionanopark Ltd. is a non-profit research institution providing employment for two of the authors [JG, JAB], whose facilities were used for part of the conducted studies. The funder provided support in the form of research materials, but did not have any additional role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript.pl_PL
dc.publisherPublic Library of Sciencepl_PL
dc.relation.ispartofseriesPLoS ONE;13(1)
dc.rightsUznanie autorstwa 4.0 Międzynarodowe*
dc.subjectbinding analysispl_PL
dc.subjecttransmission electron microscoppl_PL
dc.subjectisothermal titration calorimetrypl_PL
dc.subjectAlzheimer's diseasepl_PL
dc.titleFunctional consequences of piceatannol binding to glyceraldehyde-3-phosphate dehydrogenasepl_PL
dc.contributor.authorAffiliationDepartment of Molecular Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Polandpl_PL
dc.contributor.authorAffiliationDepartment of Molecular Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Polandpl_PL
dc.contributor.authorAffiliationBionanopark Ltd., Lodz, Polandpl_PL
dc.contributor.authorAffiliationUnit of Biophysical Chemistry, Department of Physical Chemistry, Faculty of Chemistry, University of Lodz, Lodz, Polandpl_PL
dc.contributor.authorAffiliationLaboratory of Computer and Analytical Techniques, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Polandpl_PL
dc.contributor.authorAffiliationDepartment of General Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Polandpl_PL
dc.contributor.authorAffiliationLaboratory of Microscopic Imaging and Specialized Biological Techniques, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Polandpl_PL
dc.contributor.authorAffiliationBionanopark Ltd., Lodz, Polandpl_PL
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dc.disciplinenauki biologicznepl_PL

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Uznanie autorstwa 4.0 Międzynarodowe
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