Table 3.
Hydrophobic interactions and docked amino acid residues of albumin with EC, ECG, EGC, EGCG and (+)- catechin
| Ligand | Protein | Binding Energy | Ligand efficiency | Intermole energy | Ligand atoms |
Docked amino
Acid residue(bond length) |
|---|---|---|---|---|---|---|
| EC | Casein | -3.25 | -0.1 | -4.79 | C-7’ OH | A-Met 115/HN (2.9 A⁰) |
| ECG | Casein | -3.44 | -0.11 | -5.15 | D-6’ OH D-7’ OH |
A-Pro 116/O (2.6, 2.2 A⁰) |
| EGC | Casein | -3.39 | -0.15 | -4.25 | A-3’OH B-4’ OH |
A-Met 115/O (1.8 A⁰) A-Pro 116/O (1.7 A⁰) |
| EGCG | Casein | -1.67 | -0.05 | -3.88 | - | A-Ser 120/HN |
| (+)-Catechin | Casein | -3.3 | -0.16 | -4.38 | B-2’ OH B-3’ OH |
A-Pro 116/O (2.0, 2.1 A⁰) |