TY - JOUR
T1 - Triazoloquinazolines as a new class of potent α-glucosidase inhibitors
T2 - In vitro evaluation and docking study
AU - Abuelizz, Hatem A.
AU - Anouar, El Hassane
AU - Ahmad, Rohaya
AU - Nor Azman, Nor Izzati Iwana
AU - Marzouk, Mohamed
AU - Al-Salahi, Rashad
N1 - Publisher Copyright:
© 2019 Abuelizz et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
PY - 2019/8/1
Y1 - 2019/8/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85070667230&partnerID=8YFLogxK
U2 - 10.1371/journal.pone.0220379
DO - 10.1371/journal.pone.0220379
M3 - Article
C2 - 31412050
AN - SCOPUS:85070667230
SN - 1932-6203
VL - 14
JO - PLoS ONE
JF - PLoS ONE
IS - 8
M1 - e0220379
ER -