Binding and Anticancer Properties of Plumbagin with Human Serum Albumin |
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| Authors: | Yi Gou Yao Zhang Jinxu Qi Linlin Kong Zuping Zhou Shichu Liang Feng Yang Hong Liang |
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| Affiliation: | 1. State Key Laboratory Cultivation Base for the Chemistry and Molecular Engineering of Medicinal Resources, Ministry of Science and Technology of China, Guangxi Normal University, 15 Yucai Road Guilin, Guangxi, China;2. Key Laboratory of Ecology of Rare an Endangered species and Environmental Protection, Ministry of Education of the People's Republic of China, Guangxi Normal University, 15 Yucai Road Guilin, Guangxi, China |
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| Abstract: | Plumbagin has received extensive attention as a promising anticancer drug. Therefore, we investigated the binding and anticancer properties of plumbagin with human serum albumin. Fluorescence results demonstrated that plumbagin interacts with human serum albumin, although its binding affinity may be affected to various extents by different compounds. The human serum albumin–plumbagin complex structure revealed that plumbagin binds to the hydrophobic cavity in the IIA subdomain of human serum albumin through hydrogen bonding and hydrophobic interactions. The plumbagin–human serum albumin complex enhances cytotoxicity by 2‐ to 3‐fold particularly in cancer cells but has no effect on normal cells in vitro. Compared with the unbound drug, the human serum albumin–plumbagin complex promotes HeLa cell apoptosis and has a stronger capacity for cell cycle arrest at the G2/M phase of HeLa cells. In conclusion, this study contributes to the rational design and development of plumbagin‐based drugs and a drug–human serum albumin delivery system. |
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| Keywords: | anticancer activity drug carrier human serum albumin plumbagin protein complex structure |
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