Triazoloquinazolines as a new class of potent α-glucosidase inhibitors: in vitro evaluation and docking study

Hatem A Abuelizz; El Hassane Anouar; Rohaya Ahmad; Nor Izzati Iwana Nor Azman; Mohamed Marzouk; Rashad Al-Salahi

doi:10.1371/journal.pone.0220379

Triazoloquinazolines as a new class of potent α-glucosidase inhibitors: in vitro evaluation and docking study

PLoS One. 2019 Aug 14;14(8):e0220379. doi: 10.1371/journal.pone.0220379. eCollection 2019.

Authors

Hatem A Abuelizz¹, El Hassane Anouar², Rohaya Ahmad³, Nor Izzati Iwana Nor Azman³, Mohamed Marzouk⁴, Rashad Al-Salahi¹

Affiliations

¹ Department of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, Riyadh, Saudi Arabia.
² Department of Chemistry, College of Sciences and Humanities, Prince Sattam bin Abdulaziz University, Al Kharj, Saudi Arabia.
³ Faculty of Applied Sciences, Universiti Teknologi MARA, shah Alam, Selangor Darul Ehsan, Malaysia.
⁴ Chemistry of Natural Products Group, Centre of Excellence for Advanced Sciences, National Research Centre, Dokki, Cairo, Egypt.

Abstract

Previously, we synthesized triazoloquinazolines 1-14 and characterized their structure. In this study, we aimed to evaluate the in vitro activity of the targets 1-14 as α-glucosidase inhibitors using α-glucosidase enzyme from Saccharomyces cerevisiae type 1. Among the tested compounds, triazoloquinazolines 14, 8, 4, 5, and 3 showed the highest inhibitory activity (IC50 = 12.70 ± 1.87, 28.54 ± 1.22, 45.65 ± 4.28, 72.28 ± 4.67, and 83.87 ± 5.12 μM, respectively) in relation to that of acarbose (IC50 = 143.54 ± 2.08 μM) as a reference drug. Triazoloquinazolines were identified herein as a new class of potent α-glucosidase inhibitors. Molecular docking results envisaged the plausible binding interaction between the target triazoloquinazolines and α-glucosidase enzyme and indicated considerable interaction with the active site residues.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Glycoside Hydrolase Inhibitors / pharmacology*
Molecular Docking Simulation*
Molecular Structure
Quinazolines / pharmacology*
Saccharomyces cerevisiae / metabolism
Structure-Activity Relationship
Triazoles / pharmacology*
alpha-Glucosidases / metabolism*

Substances

Glycoside Hydrolase Inhibitors
Quinazolines
Triazoles
triazoloquinazoline
alpha-Glucosidases

Grants and funding

The authors extend their appreciation to the Deanship of Scientific Research at King Saud University for funding this study through research group no. RG-1435–068.