Phytochemical Analysis, Biological Activities, and Docking of Phenolics from Shoot Cultures of Hypericum perforatum L. Transformed by Agrobacterium rhizogenes

Abstract

Hypericum perforatum transformed shoot lines (TSL) regenerated from corresponding hairy roots and non-transformed shoots (NTS) were comparatively evaluated for their phenolic compound contents and in vitro inhibitory capacity against target enzymes (monoamine oxidase-A, cholinesterases, tyrosinase, α-amylase, α-glucosidase, lipase, and cholesterol esterase). Molecular docking was conducted to assess the contribution of dominant phenolic compounds to the enzyme-inhibitory properties of TSL samples. The TSL extracts represent a rich source of chlorogenic acid, epicatechin and procyanidins, quercetin aglycone and glycosides, anthocyanins, naphthodianthrones, acyl-phloroglucinols, and xanthones. Concerning in vitro bioactivity assays, TSL displayed significantly higher acetylcholinesterase, tyrosinase, α-amylase, pancreatic lipase, and cholesterol esterase inhibitory properties compared to NTS, implying their neuroprotective, antidiabetic, and antiobesity potential. The docking data revealed that pseudohypericin, hyperforin, cadensin G, epicatechin, and chlorogenic acid are superior inhibitors of selected enzymes, exhibiting the lowest binding energy of ligand-receptor complexes. Present data indicate that H. perforatum transformed shoots might be recognized as an excellent biotechnological system for producing phenolic compounds with multiple health benefits.

Keywords: Hypericum perforatum; biological activities; molecular docking; phenolic compounds; transformed shoots.

Figure 1

Inhibitory activity (%) of Hypericum perforatum transformed shoot extracts against (a) momoamine oxidase-A (MAO-A), (b) acetylcholinesterase (AChE), (c) butyrylcholinesterase (BChE), (d) tyrosinase (TYR), (e) α-amylase (α-AM), (f) α-glucosidase (α-GL), (g) pancreatic lipase (PL) and (h) cholesterol esterase (CHE). NTS: non-transformed shoots, TSL B, TSL F and TSL H: transformed shoot lines, DCP: 2,4-dichlorophenol.

Figure 2

The best-ranked docking pose (a) and key interactions (b) of epicatechin in the active site of monoamine oxidase-A.

Figure 3

The best-ranked docking pose (a) and key interactions (b) of pseudohypericin in the active site of acetylcholinesterase. The best-ranked docking pose (c) and key interactions (d) of pseudohypericin in the active site of butyrylcholinesterase.

Figure 4

The best-ranked docking pose (a) and key interactions (b) of chlorogenic acid in the active site of tyrosinase.

Figure 5

The best-ranked docking pose (a) and key interactions (b) of pseudohypericin in the active site of α-amylase. The best-ranked docking pose (c) and key interactions (d) of pseudohypericin in the active site of α-glucosidase.

Figure 6

The best-ranked docking pose (a) and key interactions (b) of pseudohypericin in the active site of lipase. The best-ranked docking pose (c) and key interactions (d) of pseudohypericin in the active site of cholesterol esterase.