Table 3.
Significant results from the in silico molecular model of docking and enzyme alpha-glucosidase based on free energy of binding (ΔG), inhibitor constant of fifty percent (Ki), number of hydrogen bonds, and the length of hydrogen bonds in units of Å.
| Entry | Free Energy of Binding[a] of the best docking pose | Ki[b] | The number of hydrogen bonds[c] | The property and bond length[d] |
|---|---|---|---|---|
| NC1 |
−7.73 (Pose: 177/200) |
2.15 | 4 | A:ILE362:N–NC1:O (2.54 Å) NC1:H–A:LEU364:O (1.92 Å) NC1:H–A:ILE362:O (2.18 Å) NC1:H–A:GLN447:O (1.95 Å) |
| NC2 |
−7.03 (Pose: 106/200) |
7.08 | 8 | A:GLN447:N–NC2:O (2.96 Å) A:ASN448:N–NC2:O (3.09 Å) A:ASN448:N–NC2:O (3.14 Å) NC2:H– A:ILE362:O (2.08 Å) NC2:H–A:ASP568:O (1.73 Å) NC2:H–A:ASP568:O (2.01 Å) NC2:H–A:PHE444:O (1.94 Å) NC2:H - A:VAL446:O (2.25 Å) |
| BM3 |
−6.73 (Pose: 134/200) |
11.72 | 7 | A:ARG428:N–BM3:O (2.64 Å) A:ARG428:N–BM3:O (3.11 Å) BM3:H– A:ILE362:O (2.20 Å) BM3:H– A:ILE362:O (2.34 Å) BM3:H–A:GLN447:O (1.97 Å) BM3:H–A:GLN447:O (1.96) BM3:H–A:GLU429:O (2.09) |
| Acarbose |
−6.54 (Pose: 52/200) |
15.98 | 12 | A:ARG428:N–Acarbose:O (2.84 Å) Acarbose :H–A:VAL446:O (2.28 Å) Acarbose:H–A:VAL446:O (2.36 Å) Acarbose :H–A:GLU443:O (2.28 Å) Acarbose:H–A:GLU443:O (2.26 Å) Acarbose:H–A:GLN445:O (2.01 Å) Acarbose:H–A:GLN442:O (2.18 Å) Acarbose:H–A:GLN442:O (2.01 Å) Acarbose:H - A:LEU364:O (2.20 Å) Acarbose :H - A:GLU443:O (2.06 Å) Acarbose:H–A:GLU443:O (1.95 Å) Acarbose :H–A:ILE362:O (1.82 Å) |
[a]. Calculated using AutoDockTools–1.5.6rc3 and reported in units of kcal.mol−1. [b]. Inhibition constants Ki, µM derived using AutoDockTools–1.5.6rc3. [c],[d]. Based on Discovery Studio (DSC) software.