Glycyrrhizic Acid Scavenges Reactive Carbonyl Species and Attenuates Glycation-Induced Multiple Protein Modification: An <i>In Vitro</i> and <i>In Silico</i> Study

<div>Molecular binding of D-ribose, GA, and AG with BSA (PDB ID: 4F5S). (a) Binding of GA (<i>Δ</i>G: -8.8 Kcal/mol), AG (<i>Δ</i>G: -4.3 Kcal/mol), and D-ribose (<i>Δ</i>G: -5.2 Kcal/mol) in the binding pocket of BSA while BSA has been represented as hydrophobic surface. (b) Enlarged view of interaction of D-ribose, GA, and AG with the interacting residues of BSA.</div>

Oxidative Medicine and Cellular Longevity

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Figure 8

Figure 8: Glycyrrhizic Acid Scavenges Reactive Carbonyl Species and Attenuates Glycation-Induced Multiple Protein Modification: An <i>In Vitro</i> and <i>In Silico</i> Study 

Figure 8 | Glycyrrhizic Acid Scavenges Reactive Carbonyl Species and Attenuates Glycation-Induced Multiple Protein Modification: An In Vitro and In Silico Study 