## 3 Results and Discussion
### Molecular Docking Studies  
A set of 22 characteristic phenolic compounds (Figure 2), abundant in the studied edible flowers, was generated for further exploration. This comprised phenolic acids, stilbenes, flavanols, flavanones and flavonoids [5; 31; 32; 44]. Figure 2: The chemical structures of the examined phenolic compounds. The molecular target selection was based on the inhibition of reactive oxygen species (ROS) overproduction which negatively affects antioxidant activity. Therefore, five enzymes that are responsible for reactive oxygen species (ROS) production during metabolism, NADPH oxidase (PDB: 2 CDU), cytochrome P450 (CP450) (PDB: 1 OG5), lipoxygenase (LOX) (PDB: 1N8Q), myeloperoxidase (MP) (PDB: 1 DNU) and xanthine oxidase (XO) (PDB: 3 NRZ) enzymes, were utilized for docking studies [23; 26]. Additionally, dextromethorphan (DEX), 5-fluorouracil (FLU), zileuton (ZIL), melatonin (MEL) and febuvostat (FEB) were utilized as positive controls against NO, CP450, LOX, MP and XO enzymes, respectively, and were subjected to docking studies. Representative binding poses of phenolic compounds at the binding sites of NADPH oxidase, CP450, LOX, MP and XO enzymes are illustrated in Figure 3.  
Analysis of the docking results indicated that the tested molecules exhibited similar or greater binding energy values compared to positive controls at all targets, ranging from \(-9.00\) kcal\(\cdot\)mol\({}^{-1}\) to \(-4.00\) kcal\(\cdot\)mol\({}^{-1}\) (Table 4). Therefore, the evaluation of docking poses was based not only on docking scores but also on the common interactions between the co-crystallized ligands and positive controls. The interactions of positive controls, co-crystallized ligands and examined phytochemicals for each enzyme target are illustrated in Table 5. It is critical to highlight that the presented interactions are in accordance with the results of recent published studies [23; 24]. In general, the visual inspection of the derived docking poses revealed that the examined compounds are stabilized into the binding pockets of the enzymes via the formation of hydrogen bonds and by pi-pi and pi-c interactions. However, several phenolic compounds did not seem to bind to lipoxygenase (LOX) and xanthine oxidase (XO) enzymes, probably due to steric hindrances. In contrast, all of the compounds exhibited binding capacity to NADPH oxidase, cytochrome P450 (CP450) and myeloperoxidase (MP) enzymes and could potentially inhibit ROS reproduction, thus providing oxidative stress reduction. In the case of the NADPH oxidase enzyme, docking results showed a significantly higher binding affinity for all tested compounds compared to the positive control DEX. Additionally, docking poses indicated that all phenolic acids included in the set form direct hydrogen bonds with Asp179 and/or Val214, similar to the co-crystallized ligand and the positive control. The group of flavanols presents a common interaction pattern, including  
Figure 3: Representative binding poses of (**a**) cafratic acid, (**b**) naringin, (**c**) vanillic acid, (**d**) kaem-phenyl 3-glucoside and (**e**) resveratrol, derived from molecular docking studies of NADPH oxidase, CP450, LOX, MP and XO enzymes. Hydrogen bonds are depicted with dashed yellow lines and pi–pi interactions with dashed blue lines. crucial interactions, such as hydrogen bonds with Asp179 and Val214. Additionally, it was observed that within the group of flavonoids, rutin, kaempfer 3-glucoside and myricetin present similar interaction patterns, including interactions with Lys213 and Val214, while quercetin 3-glucoside is capable of a variety of interactions and direct hydrogen bonding with Asp179. Furthermore, the aglycones hesperetin and naringenin present the same interaction motif, different from their glucosides. The above-mentioned interactions have been found to be positively correlated with increased (predicted) antioxidant activity in recent publications [23; 24; 45].