@article { author = {Taherkhani, Amir and Moradkhani, Shirin and Orangi, Athena and Jalalvand, Alireza and Khamverdi*, Zahra}, title = {In silico Study of Some Natural Anthraquinones on Matrix Metalloproteinase Inhibition}, journal = {Research Journal of Pharmacognosy}, volume = {8}, number = {4}, pages = {37-51}, year = {2021}, publisher = {- The Iranian Society of Pharmacognosy - Shahid Beheshti University of Medical Sciences}, issn = {2345-4458}, eissn = {2345-5977}, doi = {10.22127/rjp.2021.288366.1705}, abstract = {Background and objectives: Matrix metalloproteinase-13 (MMP-13) is a proteolytic enzyme playing an important role in the activation of the MMP cascade, which seems to be vital in both bone metabolism and homeostasis. However, the up-regulation of MMP-13 is involved in developing several human disorders such as aggressive tumors, tooth decay, rheumatoid arthritis, osteoarthritis, skin ageing, and Alzheimer's disease. We performed a molecular docking analysis to discover the potential MMP-13 inhibitors in a total of 21 anthraquinone derivatives. Methods: The binding affinity of the tested compounds to the MMP-13 catalytic site was estimated by the Autodock 4.0 software. Moreover, the stability of the docked pose of the top-ranked compounds were examined using molecular dynamics simulations. Results: Pulmatin, sennidin A, emodin-8-glucoside, emodin, rhodoptilometrin, chrysophanol, knipholone, sennidin B, aloe emodin 8-glucoside, and aloe-emodin demonstrated considerable binding affinity to the MMP-13 active site. However, the molecular dynamics simulations showed that the docked poses of sennidin A and sennidin B were not considerably stable. Conclusion: The present study suggested that pulmatin, emodin-8-glucoside, emodin, rhodoptilometrin, chrysophanol, knipholone, aloe emodin 8-glucoside, and aloe-emodin may be considered as drug candidates for therapeutic applications in many human diseases. However, the validation of this finding is needed in the future.}, keywords = {Anthraquinones,cancer,matrix metalloproteinase-13,MMP inhibitor,Molecular docking}, url = {https://www.rjpharmacognosy.ir/article_135900.html}, eprint = {https://www.rjpharmacognosy.ir/article_135900_2443166e7219a261f7d8c529936ea219.pdf} }