Phenolic Composition, Antioxidant Properties, and Inhibition toward Digestive Enzymes with Molecular Docking Analysis of Different Fractions from Prinsepia utilis Royle Fruits

Abstract

The present study investigated the phenolic profiles and antioxidant properties of different fractions from Prinsepia utilis Royle fruits using molecular docking analysis to delineate their inhibition toward digestive enzymes. A total of 20 phenolics was identified and quantified. Rutin, quercetin-3-O-glucoside, and isorhamnetin-3-O-rutinoside were the major phenolic compounds in the total phenolic fraction and flavonoid-rich fraction. The anthocyanin-rich fraction mainly contained cyanidin-3-O-glucoside and cyanidin-3-O-rutinoside. All of the fractions exhibited strong radical scavenging activities and good inhibition on cellular reactive oxygen species (ROS) generation in H2O2-induced HepG2 cells, as evaluated by DPPH and 2,2′-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) assays. Moreover, the powerful inhibitory effects of those fractions against pancreatic lipase and α-glucosidase were observed. The major phenolic compounds that were found in the three fractions also showed good digestive enzyme inhibitory activities in a dose-dependent manner. Molecular docking analysis revealed the underlying inhibition mechanisms of those phenolic standards against digestive enzymes, and the theoretical analysis data were consistent with the experimental results.

HPLC-ESI-qTOF-MS/MS Characterization, Antioxidant Activities and Inhibitory Ability of Digestive Enzymes with Molecular Docking Analysis of Various Parts of Raspberry (Rubus ideaus L.)

“…Hua et al (2018) have also reported that Asp 69, Asp 215, and Arg 442 were the important residues involved in H-bond formation during the binding with α-glucosidase [37]. also reported that the binding active sites (Asp 215 and Asp 352) in between the ligands and α-glucosidase played important roles in exert its α-glucosidase inhibitory effect [23]. Similarly, the order of amino acid residues numbers formed by four molecules (GA, EA, PC, and Acarbose) docked with α-amylase was: Acarbose (7) = PC (7) > GA (5) > EA (4).…”

“…The correlation analysis results between the TPC and two digestive enzymes inhibition potency clearly verified that there was a good positive correlation between these two parameters (α-glucosidase inhibition potency vs. TPC, r = 0.781, p < 0.05; α-amylase inhibition potency vs. TPC, r = 0.854, p < 0.01). Many researches have confirmed that phenolic-rich extracts from leaf-tea, edible fruits, and natural products possess good inhibitory ability on digestive enzymes [23,37]. have confirmed that procyanidin C3 possessed strong α-glucosidase inhibitory capacity [38].…”

“…The 2D conformers of the main phenolic standards (gallic acid, ellagic acid, and procyanidin C3) and acarbose (an anti-diabetic drug) were drawn by Chem 3D software, and the PDB formats of the α-glucosidase (PDB ID:3A4A) and α-amylase (PDB ID:1PPI) were downloaded from RCSB PDB (http://www.rcsb.org/pdb/home/home.do) [23]. Because the structural information of α-glucosidase from S. cerevisiae was not available, the homology structural (isomaltase, PDB ID: 3A4A) with high similarity of α-glucosidase was used as the template to perform the α-glucosidase docking analysis [23]. The molecular docking analysis of the main phenolic standards and acarbose to digestive enzymes was performed by the Surflex-Dock Geom (SFXC) mode using SYBYL-X 2.0 software package (Tripos, Inc., St. Louis, MO, USA).…”

Inhibición de lipasa pancreática por flavonoides: importancia del doble enlace C2=C3 y la estructura plana del anillo C//Inhibition of pancreatic lipase by flavonoids: relevance of the C2=C3 double bond and C-ring planarity

“…Esto concuerda con el análisis de docking realizado para el pNPL (Figura 4a). Mientras que el sitio para RUT, diferente al del resto de los flavonoides, se encuentra ubicado en una región comprendida entre el sitio activo y la colipasa (Zhang et al, 2018). La inhibición mixta observada para la mayoría de los flavonoides, indica que los flavonoides se unen al enzima antes y después de que el sustrato esté unido (Birari et al, 2011;Li et al, 2011).…”

“…La estructura plana del anillo C de LUT y QUE les permite ingresar e interactuar con los residuos de aminoácidos del sitio activo (Cerezo et al, 2015). En este sentido, la mayoría de los flavonoides interactúan con el subsitio 1 (mayor actividad) de los tres sitios descritos por otros autores, y RUT con el subsitio 3, ambos hidrofóbicos (Zhang et al, 2018). Se señala que el Orlistat se une a los tres subsitios e impide el ingreso del sustrato.…”