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