Molecular Docking Study of Curcumin vs. Polydatin on the Protein Kinase Family

Protein kinases play central roles in cellular signaling pathways, and their dysregulation is implicated in numerous diseases, including cancer, inflammation, and cardiovascular disorders. Natural compounds such as curcumin and polydatin have demonstrated potential in modulating kinase activity, but a systematic comparison of their interactions with protein kinases has not been extensively explored. In this study, we performed a comprehensive molecular docking analysis of curcumin and polydatin against 77 protein kinases, including receptor and non-receptor tyrosine kinases, using AutoDock Vina via the PyRx platform. Our results indicate that polydatin generally exhibits stronger binding affinities across a broad range of kinases compared to curcumin, with particularly high affinities observed for ABL1, DDR1, FGFR3, TNNI3K, JAK1, and JAK2. In contrast, curcumin shows selective strong binding primarily to KIT and DDR1. These findings highlight polydatin’s potential as a multi-target therapeutic agent, capable of modulating key kinases involved in cancer, inflammation, and cardiovascular disease. The study provides a foundation for further in vitro and in vivo investigations into polydatin as a promising candidate for targeted kinase inhibition and therapeutic development.