Epo-C12 inhibits peroxiredoxin 1 peroxidase activity

Epo-C12 is a synthetic derivative of epolactaene, isolated from Penicillium sp. BM 1689-P. Epo-C12 induces apoptosis in human acute lymphoblastoid leukemia BALL-1 cells. In our previous studies, seven proteins that bind to Epo-C12 were identified by a combination of pull-down experiments using biotinylated Epo-C12 (BioEpo-C12) and mass spectrometry. In the present study, the effect of Epo-C12 on peroxiredoxin 1 (Prx 1), one of the proteins that binds to Epo-C12, was investigated. Epo-C12 inhibited Prx 1 peroxidase activity. However, it did not suppress its chaperone activity. Binding experiments between Bio-Epo-C12 and point-mutated Prx 1s suggest that Epo-C12 binds to Cys52 and Cys83 in Prx 1. The present study revealed that Prx 1 is one of the target proteins through which Epo-C12 exerts an apoptotic effect in BALL-1 cells.

Automated summary

Epo-C12, a synthetic derivative of epolactaene isolated from Penicillium sp. BM 1689-P, induces apoptosis in BALL-1 cells. The study reveals that Epo-C12 inhibits peroxidase activity of Prx 1 without affecting its chaperone activity. Epo-C12 binds to Cys52 and Cys83 in Prx 1, indicating Prx 1 as a target protein for Epo-C12-induced apoptotic effect in BALL-1 cells.