in silico study of some natural anthraquinones on matrix metalloproteinase inhibition

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.