Phenolic Profile, Antioxidant and Enzyme Inhibitory Activities of Leaves from Two Cassia and Two Senna Species

Abstract

Several species within the genera Cassia or Senna have a treasure of traditional medicines worldwide and can be a promising source of bioactive molecules. The objective of the present study was to evaluate the phenolic content and antioxidant and enzyme inhibition activities of leaf methanolic extracts of C. fistula L., C. grandis L., S. alexandrina Mill., and S. italica Mill. The two Cassia spp. contained higher total polyphenolic content (42.23–49.75 mg GAE/g) than the two Senna spp., and C. fistula had significantly (p ˂ 0.05) the highest concentration. On the other hand, the Senna spp. showed higher total flavonoid content (41.47–59.24 mg rutin equivalent per g of extract) than that found in the two Cassia spp., and S. alexandrina significantly (p ˂ 0.05) accumulated the highest amount. HPLC–MS/MS analysis of 38 selected bioactive compounds showed that the majority of compounds were identified in the four species, but with sharp variations in their concentrations. C. fistula was dominated by epicatechin (8928.75 µg/g), C. grandis by kaempferol-3-glucoside (47,360.04 µg/g), while rutin was the major compound in S. italica (17,285.02 µg/g) and S. alexandrina (6381.85). The methanolic extracts of the two Cassia species exerted significantly (p ˂ 0.05) higher antiradical activity, metal reducing capacity, and total antioxidant activity than that recorded from the two Senna species’ methanolic extracts, and C. fistula displayed significantly (p ˂ 0.05) the highest values. C. grandis significantly (p ˂ 0.05) exhibited the highest metal chelating power. The results of the enzyme inhibition activity showed that the four species possessed anti-AChE activity, and the highest value, but not significantly (p ≥ 0.05) different from those obtained by the two Cassia spp., was exerted by S. alexandrina. The Cassia spp. exhibited significantly (p ˂ 0.05) higher anti-BChE and anti-Tyr properties than the Senna spp., and C. grandise revealed significantly (p ˂ 0.05) the highest values. C. grandise revealed significantly (p ˂ 0.05) the highest α- amylase inhibition, while the four species had more or less the same effect against the α-glucosidase enzyme. Multivariate analysis and in silico studies showed that many of the identified phenols may play key roles as antioxidant and enzyme inhibitory properties. Thus, these Cassia and Senna species could be a promising source of natural bioactive agents with beneficial effects for human health.

Essential Oils Composition and Biological Activity of Chamaecyparis obtusa, Chrysopogon nigritanus and Lavandula coronopifolia Grown Wild in Sudan

“…The details of the homology modeling are available in the Ref. [ 56 ]. All protein structures were prepared according to the protocol described in the Ref.…”

Phytochemical Screening, Antioxidant Activity, and Acute Toxicity Evaluation of Senna italica Extract Used in Traditional Medicine

“…Means with letters a; b; c in the same row are diferent (p < 0.05); Means with * ; * * ; * * * in the same column are diferent for D0 and D14 of the same parameter. * � p < 0.05; * * � p < 0.01; * * * � p < 0.001. attributed to them[23]. Te study showed that the aqueous extract (p < 0.001) has the highest proportion of total phenol (1497.24% ± 21.55) and of favonoids (1278.11% ± 21.23) (p < 0.0001).…”

Novel Signposts on the Road from Natural Sources to Pharmaceutical Applications: A Combinative Approach between LC-DAD-MS and Offline LC-NMR for the Biochemical Characterization of Two Hypericum Species (H. montbretii and H. origanifolium)

“…However, the crystal structures of human tyrosinase and glucosidase are not available; therefore, Priestia megaterium tyrosinase (PDB ID: 6QXD) [ 82 ] and Mus musculus alpha-glucosidase (PDB ID: 7KBJ) [ 83 ] were retrieved and used as templates to build their human models using the respective human sequences and UniProt entries P14679 and P0DUB6. The detailed procedure of the model building was described previously in [ 84 ]. The pKa of titratable residues in each protein was predicted using the “Playmolecule ProteinPrepare” module [ 85 ] and was then used to prepare the proteins at a physiological pH of 7.4.…”