Abstract
1,4-Disubstituted-1,2,3-triazoles were synthesized by Cu(I) catalyzed click reaction, where the azides, with electron donating and electron withdrawing groups acted as 1,3-dipoles and 1-ethynyl-1-cyclohexanol served as the terminal alkyne. These synthesized triazoles were subjected to enzymatic assay which showed promising activity against α-glucosidase; 1-(2-cyano-4-nitrophenyl)-4-(1-hydroxycyclohexyl)-1H-1,2,3-triazole 3m being the most active members of the library. Molecular docking studies of these triazoles with the homology-modeled α-glucosidase protein were also performed to delineate ligand-protein interactions at molecular level which suggested that Phe157, Arg312 and His279 are the major interacting residues in the biding site of the protein and may have a significant role in the inhibition of enzyme's function.
Original language | English (US) |
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Pages (from-to) | 1029-38 |
Number of pages | 10 |
Journal | Bioorganic and Medicinal Chemistry Letters |
Volume | 26 |
Issue number | 3 |
DOIs | |
State | Published - Feb 1 2016 |
Keywords
- Amino Acid Sequence
- Bacillus cereus
- Binding Sites
- Catalytic Domain
- Click Chemistry
- Glycoside Hydrolase Inhibitors
- Hydrogen Bonding
- Molecular Docking Simulation
- Molecular Sequence Data
- Saccharomyces cerevisiae
- Sequence Alignment
- Structure-Activity Relationship
- Triazoles
- alpha-Glucosidases
- Journal Article
- Research Support, Non-U.S. Gov't