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

Figure 5

(a, A) GA preserves the secondary structures in D-ribose-mediated protein glycation. Far UV CD (190-260 nm) spectra of native BSA, Gly-BSA, and GA-treated Gly-BSA samples. The spectra are the of three determinations. The results are represented as change in ellipticity (mdeg) of Gly-BSA either in the presence or absence of GA. (a, B) The % α-helix and β-sheet content of native BSA, Gly-BSA, and GA-treated Gly-BSA. % α-helix and β-sheet content was interpreted through K2D2 software (http://cbdm-01.zdv.uni-mainz.de/~andrade/k2d2/). Values (% α-helix and β-sheet content) are the of three determinations. Significant difference vs. native BSA at ^###. Significant difference vs. Gly-BSA at . (b, A) AG preserves the secondary structures in D-ribose-mediated protein glycation. Far UV CD (190-260 nm) spectra of native BSA, Gly-BSA, and AG-treated Gly-BSA samples. The spectra are the of three determinations. The results are represented as change in ellipticity (mdeg) of Gly-BSA either in the presence or absence of AG. (b, B) The % α-helix and β-sheet content of native BSA, Gly-BSA, and AG-treated Gly-BSA. Values (% α-helix and β-sheet content) are the of three determinations. Significant difference vs. native BSA at ^###. Significant difference vs. Gly-BSA at .

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