Inhibition of N-terminal lysines acetylation and transcription factor assembly by epirubicin induced deranged cell homeostasis.

摘要: Epirubicin (EPI), an anthracycline antitumour antibiotic, is a known intercalating and DNA damaging agent. Here, we study the molecular interaction of EPI with histones other cellular targets. binding histone core protein was predicted spectroscopic computational techniques. The distance r, between donor (histone H3) acceptor (EPI) estimated using Forster's theory non-radiation energy transfer detailed phenomenon expounded. Interestingly, concentration dependent reduction in acetylated states H3 K9/K14 observed suggesting more repressed chromatin state on treatment. Its site near N-terminal lysines further characterized by thermodynamic determinants docking studies. Specific inhibition transcription factor (Tf)-DNA complex formation implicates induced transcriptional inhibition. also showed significant cell cycle arrest drug treated cells. Chromatin fragmentation loss membrane integrity cells suggestive their commitment to death. This provides analysis nucleosome dynamics during treatment novel insight into its action.