In vitro α-amylase and hemoglobin glycation inhibitory potential of Nigella sativa essential oil, and molecular docking studies of its principal components

Abstract

Nigella sativa is plant that is endowed with various pharmacological activities including antioxidant, anticancer, anti-inflammatory, antibacterial, antidiabetic, and immunostimulant. This study aims to investigate the antidiabetic activity of the N. sativa essential oil on two key enzymes the α-amylase and hemoglobin glycation. After the extraction procedure, the N. sativa essential oil, were subject to qualitative and semi-quantitative analysis using GC/MS, for the identification of the different bioactive compounds. This was followed by an evaluation of the in vitro inhibition capacity of the α-amylase and the hemoglobin glycation. Finally, a molecular docking study was conducted to determine the bioactive compounds responsible for the antidiabetic activity. The extracted essential oil showed the presence of different bioactive compounds including α-phellandrene (29.6%), β-cymene (23.8%), 4-caranol (9.7%), thymol (7%). The N. sativa essential oil was found to be endowed with an antiradical scavenging activity with an IC50 of (7.81 ± 0.08 mg/ml), and to have a ferric reducing activity with an IC50 value of (7.53 ± 0.11 mg/ml). The IC50 value for the α-amylase inhibitory activity was 0.809 mg/ml, indicating an inhibitory impact of the enzyme. The IC50 value for the N. sativa essential oil’s hemoglobin antiglycation activity was 0.093 mg/ml. For most predominating phytochemicals present in the N. sativa essential oil, molecular docking studies against human pancreatic α-amylase and human hemoglobin enzymes revealed that these compounds can serve as lead molecules to develop new antidiabetic compounds.

In Silico Design, Synthesis, and Evaluation of Novel Enantiopure Isoxazolidines as Promising Dual Inhibitors of α-Amylase and α-Glucosidase

“…Asp197 was proven to act as a catalytic nucleophile during starch hydrolysis; Glu233 amino acid provides an acid–base catalyst role, while Asp300 plays a leading role in optimizing the orientation of the substrate [ 49 , 50 ]. It is well reported that the redocking of the native ligand (acarbose) to the binding site of α-amylase protein (2 QV4) forms conventional hydrogen bonds with Tyr62, Gln63, Ala106, Val107, Thr163, Gly164, Arg195, His299, Asp300, and Glu233 amino acids, and Van der Waals interactions with Ile51, Trp58, Trp59, Glu60, His101, Gly104, Asn105, Tyr151, Leu162, Leu165, Asp197, Ala198, Lys200, His201, Ile235, Asn298, and His305 [ 51 ]. Thus, the binding modes of the formed complex 5d–2QV4 justify its good binding in the acarbose-binding site, sharing many similar residues.…”

D-Ribose-Induced Glycation and Its Attenuation by the Aqueous Extract of Nigella sativa Seeds

“…According to the literature, the findings showed a substantial correlation between the plant's antioxidative activities and its antiglycation capabilities. In a study by Burits and Bucar (2000) [56], the essential oil from these seeds was extracted and then analyzed using TLC for its antioxidant activity; t-Anethole, thymoquinone, terpineol, and carvacrol were discovered to have strong radical scavenging activities. The medicinal benefits of N. sativa oil and extracts have already been described.…”

Phytochemical and Biological Evaluation of a Newly Designed Vitis Vinifera Seed Oil Self-Nanoemulsifying System

“…The inhibitory effect of the α-amylase enzyme by V. vinifera seed oil and its self-nanoemulsifying formulation was evaluated using a modi ed version of a standard technique that had been previously established [34]. In order to achieve a concentration of 1000 µg/mL, the oil and its self-nanoemulsion in 10% DMSOO were dissolved individually in a buffer solution consisting of NaCl and Na2HPO4.…”