Functional consequences of piceatannol binding to glyceraldehyde-3-phosphate dehydrogenase

PloS One
Joanna GerszonAleksandra Rodacka

Abstract

Glyceraldehyde-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 analysi...Continue Reading

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Citations

Jul 30, 2019·Critical Reviews in Analytical Chemistry·Bruno Vincenzo Fiod RiccioMarlus Chorilli
Dec 20, 2020·Antioxidants·Maria-Armineh TossounianIvan Gout
Sep 9, 2020·European Journal of Medicinal Chemistry·Andrea GalbiatiPaola Conti
Apr 22, 2020·The Journal of Organic Chemistry·Guillaume BarbeBrian DeChristopher

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Methods Mentioned

BETA
isothermal titration calorimetry
light scattering
X-ray
transmission electron microscopy
nuclear translocation

Software Mentioned

Origin MicroCal
LigandFit
UCSF Chimera
Malvern
CDOCKER
Coolview

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