TY - JOUR
T1 - Synthesis of indole derivatives as diabetics II inhibitors and enzymatic kinetics study of α-glucosidase and α-amylase along with their in-silico study
AU - Taha, Muhammad
AU - Alrashedy, Ahlam Sayer
AU - Almandil, Noor Barak
AU - Iqbal, Naveed
AU - Anouar, El Hassane
AU - Nawaz, Muhammad
AU - Uddin, Nizam
AU - Chigurupati, Sridevi
AU - Wadood, Abdul
AU - Rahim, Fazal
AU - Das, Suprava
AU - Venugopal, Vijayan
AU - Nawaz, Faisal
AU - Khan, Khalid Mohammed
N1 - Publisher Copyright:
© 2021 Elsevier B.V.
PY - 2021/11/1
Y1 - 2021/11/1
N2 - In this study, we have investigated a series of indole-based compounds for their inhibitory study against pancreatic α-amylase and intestinal α-glucosidase activity. Inhibitors of carbohydrate degrading enzymes appear to have an essential role as antidiabetic drugs. All analogous exhibited good to moderate α-amylase (IC50 = 3.80 to 47.50 μM), and α-glucosidase inhibitory interactions (IC50 = 3.10–52.20 μM) in comparison with standard acarbose (IC50 = 12.28 μM and 11.29 μM). The analogues 4, 11, 12, 15, 14 and 17 had good activity potential both for enzymes inhibitory interactions. Structure activity relationships were deliberated to propose the influence of substituents on the inhibitory potential of analogues. Docking studies revealed the interaction of more potential analogues and enzyme active site. Further, we studied their kinetic study of most active compounds showed that compounds 15, 14, 12, 17 and 11 are competitive for α-amylase and non- competitive for α-glucosidase.
AB - In this study, we have investigated a series of indole-based compounds for their inhibitory study against pancreatic α-amylase and intestinal α-glucosidase activity. Inhibitors of carbohydrate degrading enzymes appear to have an essential role as antidiabetic drugs. All analogous exhibited good to moderate α-amylase (IC50 = 3.80 to 47.50 μM), and α-glucosidase inhibitory interactions (IC50 = 3.10–52.20 μM) in comparison with standard acarbose (IC50 = 12.28 μM and 11.29 μM). The analogues 4, 11, 12, 15, 14 and 17 had good activity potential both for enzymes inhibitory interactions. Structure activity relationships were deliberated to propose the influence of substituents on the inhibitory potential of analogues. Docking studies revealed the interaction of more potential analogues and enzyme active site. Further, we studied their kinetic study of most active compounds showed that compounds 15, 14, 12, 17 and 11 are competitive for α-amylase and non- competitive for α-glucosidase.
KW - Indole analogues
KW - Intestinal α-glucosidase enzymes interactions
KW - Kinetic study
KW - Pancreatic α-amylase
UR - http://www.scopus.com/inward/record.url?scp=85114789221&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2021.08.207
DO - 10.1016/j.ijbiomac.2021.08.207
M3 - Article
C2 - 34481854
AN - SCOPUS:85114789221
SN - 0141-8130
VL - 190
SP - 301
EP - 318
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -