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Abstract
The effects of leonurine (1) on the activity of creatine kinase (CK) have been studied. The results show that leonurine inhibits enzyme activity in concentration- and time-dependent manners (at 0.75 and 1.51 mmol from 12 to 72 h). There are two mechanisms for the inhibition process. Compound 1 first acts as a non-competitive inhibitor and then as an irreversible inhibitor. Changes of CK were not found in 10% SDS-PAGE, but the amount of dimeric CK decreased in 10% non-SDS gel. The results suggest that 1 can inhibit CK activity by degrading its dimeric structure.
Acknowledgements
The authors thank Drs Zhou Hai-Meng, Yu Zhen-Hang and Ms Wang Yu for their support during this study. This research was supported in part by the Tsinghua University–Hong Kong Baptist University Joint Institute for Research of Chinese Medicine and the Tsinghua University 985 Project.