Document Type : Original paper
Research Center for Molecular Medicine, Hamadan University of Medical Sciences, Hamadan, Iran.
Department of Pharmacognosy, School of Pharmacy, Medicinal Plants and Natural Product Research Center, Hamadan University of Medical Sciences, Hamadan, Iran.
Dental Research Center, Department of Restorative Dentistry, Dental School, Hamadan University of Medical Sciences, Hamadan, Iran.
Department of Influenza and Other Respiratory Viruses, Pasteur Institute of Iran, Tehran, Iran.
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.