Properties of substances inhibiting aggregation of oxidized GAPDH: Data on the interaction with the enzyme and the impact on its intracellular content

Vladimir F Lazarev; Alina D Nikotina; Pavel I Semenyuk; Diana B Evstafyeva; Elena R Mikhaylova; Vladimir I Muronetz; Maxim A Shevtsov; Anastasia V Tolkacheva; Anatoly V Dobrodumov; Alexey L Shavarda; Irina V Guzhova; Boris A Margulis

doi:10.1016/j.dib.2016.02.054

Properties of substances inhibiting aggregation of oxidized GAPDH: Data on the interaction with the enzyme and the impact on its intracellular content

Data Brief. 2016 Feb 27:7:524-8. doi: 10.1016/j.dib.2016.02.054. eCollection 2016 Jun.

Affiliations

¹ Institute of Cytology Russian Academy of Sciences, 194064 St. Petersburg, Russia.
² Belozersky Institute of Physico-Chemical Biology of Moscow State University, 119992 Moscow, Russia.
³ Institute of Macromolecular Compounds Russian Academy of Sciences, 199004 St. Petersburg, Russia.
⁴ Komarov Botanical Institute Russian Academy of Sciences, 197376 St. Petersburg, Russia.

Abstract

This data is related to our paper "Small molecules preventing GAPDH aggregation are therapeutically applicable in cell and rat models of oxidative stress" (Lazarev et al. [1]) where we explore therapeutic properties of small molecules preventing GAPDH aggregation in cell and rat models of oxidative stress. The present article demonstrates a few of additional properties of the chemicals shown to block GAPDH aggregation such as calculated site for targeting the enzyme, effects on GAPDH glycolytic activity, influence on GAPDH intracellular level and anti-aggregate activity of pure polyglutamine exemplifying a denatured protein.