and secondary metabolites exhibit neuroprotective potential: insights from in vitro, ex vivo and computational models.

Cinnamon and coriander plants are sources of popular spice products in different cuisines prepared by many people worldwide. The inhibitory effect of cinnamon bark and coriander seeds aqueous extracts on butyrylcholinesterase (BChE) and acetylcholinesterase (AChE) activities, and their antioxidant properties were investigated using in vitro, molecular docking and molecular dynamics (MD) computational models. Standard experimental methods were employed to determine the plant extracts' antioxidant and enzyme-inhibitory capacities. Subsequently, chemically annotated metabolites from the extracts were subjected to MD with the enzymes before the ligand-protein complexes of two compounds with the highest docking scores were subjected to MD at 300 ns. Phytochemical profiling of extracts from the plants via Gas Chromatography-Mass Spectrometry analysis revealed the presence of polyphenols, flavonoids, terpenes and their derivatives. The extracts from the plant inhibited the investigated cholinergic proteins, although no significant differences ( > 0.05) were observed in the IC values for their activities. While both extracts demonstrated good antioxidative activities, the cinnamon extract exhibited better radical scavenging and Fe-chelation abilities, while the coriander extract exhibited superior ferric-reducing properties. Amongst the chemical compounds identified from the plants' extract, chlorogenic acid with - 31.87 kcal/mol & - 39.29 kcal/mol and rutin with - 48.27 kcal/mol & - 54.37 kcal/mol MM/GBSA computed scores exhibited more negative binding affinity, thus showed potential to be the dominant inhibitors of the AChE and BChE enzymes, respectively. The 300 ns MD results revealed that the proteins' structure was stable after binding of the spice phytoconstituents. Further activity-guided isolation experiment is required to determine the spices as viable sources of these neuroprotective polyphenols.