Colchicine as a potential HDAC inhibitor: comparative binding energies and prospects for cancer therapy repurposing

Drug repurposing, also known as drug repositioning or drug reprofiling, is gaining momentum as a strategy to identify novel therapeutic uses for existing drugs outside their original medical indications. This approach leverages the known safety profiles and mechanisms of action of approved medications to expedite the development of treatments for various diseases. Colchicine, an ancient herbal medicine with established anti-inflammatory properties and recognized efficacy in conditions like gout and Familial Mediterranean fever, has garnered interest in its potential applications beyond traditional uses. The discovery of colchicine's binding capacity to microtubules, essential for cellular structure and mitosis, has sparked exploration into its role in cancer therapy. Histone deacetylase inhibitors (HDACs) have also shown promise in cancer research by modulating gene expression through histone and non-histone protein acetylation. While colchicine is not conventionally classified as an HDAC inhibitor, studies suggest its potential impact on HDAC activity. This study aims to investigate the similarities in enzyme binding energies between colchicine and HDAC inhibitors, exploring the potential utility of colchicine as an HDAC inhibitor and introducing a new avenue for cancer treatment. By elucidating the potential therapeutic overlap between colchicine and HDAC inhibitors, this research seeks to advance the field of drug repurposing and provide novel insights into the treatment of cancer and other diseases.