Research Article
Comparison of Protective Effects of Phenolic Acids on Protein Glycation of BSA Supported by In Vitro and Docking Studies
Table 1
Molecular docking results for the interaction between phenolic acids and BSA.
| Compound | Amino acid residue | Interaction type | Distance (Å) | Binding energy (kcal mol−1) |
| Caffeic acid | Tyr 400 | Hydrogen bond | 2.91 | −7.2 | Asn 404 | Hydrogen bond | 2.59 | Leu 508 | Hydrophobic | 494 | Lys 542 | Hydrophobic | 4.50 | Met 547 | Hydrophobic | 4.40 | Phe 550 | Hydrophobic | 3.85 |
| Ellagic acid | Glu 424 | Electrostatic | 4.71, 4.55 | −8.7 | Ser 428 | Hydrogen bond | 3.23 | Ala 193 | Hydrophobic | 3.81, 4.34, 5.29, 5.39 | Arg 196 | Hydrophobic | 5.39, 4.79 | Arg 458 | Electrostatic, hydrophobic | 4.9, 4.15, 3.51, 4.27 | His 145 | Hydrophobic | 2.0 | Arg 144 | Hydrogen bond | 2.94 |
| Ferulic acid | Ala 527 | Hydrogen bond | 2.90 | −6.9 | Phe 550 | Hydrophobic | 3.92 | Thr 578 | Hydrophobic | 4.20 |
| Gallic acid | Tyr 400 | Hydrogen bond | 3.05, 3.22 | −6.3 | Asn 404 | Hydrogen bond | 2.98, 3.23 | Leu 527 | Hydrophobic | 2.19, 4.39 | Met 547 | Hydrophobic | 4.32 | Lys 524 | Hydrogen bond, hydrophobic | 2.36, 4.58 |
| p-Coumaric acid | Leu 531 | Hydrophobic | 5.01 | −7.1 | Phe 506 | Hydrophobic | 4.52 | Val 575 | Hydrogen bond | 3.78 |
| Synergic acid | Ile 289 | Hydrophobic | 4.78 | −6.5 | Ala 290 | Hydrogen bond | 3.58 | His 241 | Hydrogen bond | 3.58 | Leu 237 | Hydrophobic | 4.99 | Arg 256 | Hydrogen bond | 3.03, 3.13 |
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