Abstract
Seven ent-kaurane diterpenoids from Croton tonkinensis were tested for cytotoxicity against human HCC HepG2 cell line. The abrogation of mortalin-p53 interaction represent an original anticancer therapeutic approach. Teritary structure of protein mortalin was constructed using Protein Structure Prediction Server and crystal structure of p53 was selected from Protein Data Bank involving mortalin-p53 binding domain. Molecular docking studies revealed that the interaction with protein mortalin is more prominent than p53 compound 5 and 1 as the most two potential mortalin-p53 binding inhibitors based on binding free energy and interacting residues analysis.
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