TY - JOUR
T1 - Exploring efficacy of indole-based dual inhibitors for α-glucosidase and α-amylase enzymes
T2 - In silico, biochemical and kinetic studies
AU - Kawde, Abdel Nasser
AU - Taha, Muhammad
AU - Alansari, Raneem Saud
AU - Almandil, Noor Barak
AU - Anouar, El Hassane
AU - Uddin, Nizam
AU - Rahim, Fazal
AU - Chigurupati, Sridevi
AU - Nawaz, Muhammad
AU - Hayat, Shawkat
AU - Ibrahim, Mohamad
AU - Elakurthy, Praveen Kumar
AU - Vijayan, Venugopal
AU - Morsy, Mohamed
AU - Ibrahim, Hossieny
AU - Baig, Nadeem
AU - Khan, Khalid Mohammed
N1 - Publisher Copyright:
© 2020
PY - 2020/7/1
Y1 - 2020/7/1
N2 - α-Glucosidase and α-amylase are enzymes which are associated with diabetic II. These enzymes break macromolecules of sugar into monosugar molecules which is soluble in body, hence increase the sugar level in blood. There is need to develop economical and save inhibitors to prevent them from breaking sugar macromolecules to soluble molecules which will control the level of sugar in blood. Therefore, we synthesized indole-based derivatives (1–18) and evaluated as dual inhibitor for α-glucosidase and α-amylase. These chemical scaffolds were built with variation in aryl ring which were found active with good to moderate activity for α-glucosidase having IC50 value ranging from 13.99 ± 0.10 to 59.09 ± 0.30 μM when compared with standard acarbose with IC50 of 11.29 ± 0.10 μM; for α-amylase IC50 value ranging from 13.14 ± 0.10 to 58.99 ± 0.30 μM when compared with the standard acarbose with IC50 of 11.12 ± 0.10 μM. Structure activity relationship (SAR) has been established for all compounds. Enzymatic kinetic study and molecular docking study have been carried out to investigate the binding interactions α-glucosidase and α-amylase enzyme.
AB - α-Glucosidase and α-amylase are enzymes which are associated with diabetic II. These enzymes break macromolecules of sugar into monosugar molecules which is soluble in body, hence increase the sugar level in blood. There is need to develop economical and save inhibitors to prevent them from breaking sugar macromolecules to soluble molecules which will control the level of sugar in blood. Therefore, we synthesized indole-based derivatives (1–18) and evaluated as dual inhibitor for α-glucosidase and α-amylase. These chemical scaffolds were built with variation in aryl ring which were found active with good to moderate activity for α-glucosidase having IC50 value ranging from 13.99 ± 0.10 to 59.09 ± 0.30 μM when compared with standard acarbose with IC50 of 11.29 ± 0.10 μM; for α-amylase IC50 value ranging from 13.14 ± 0.10 to 58.99 ± 0.30 μM when compared with the standard acarbose with IC50 of 11.12 ± 0.10 μM. Structure activity relationship (SAR) has been established for all compounds. Enzymatic kinetic study and molecular docking study have been carried out to investigate the binding interactions α-glucosidase and α-amylase enzyme.
KW - Enzymatic kinetic study
KW - Indole
KW - Molecular docking
KW - α-Amylase
KW - α-Glucosidase
UR - http://www.scopus.com/inward/record.url?scp=85081729713&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2020.03.090
DO - 10.1016/j.ijbiomac.2020.03.090
M3 - Article
C2 - 32173438
AN - SCOPUS:85081729713
SN - 0141-8130
VL - 154
SP - 217
EP - 232
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -