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Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
Published on: April 5, 2022
Exploring inhibitory effect and mechanism of hesperetin-Cu (II) complex against protein glycation
1State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; Jiangxi Biotech Vocational College, Nanchang 330200, China.
Abstract:
Inhibition of advanced glycation end products (AGEs) formed in protein glycosylation is crucial for minimizing diabetic complications. Herein, the anti-glycation potential of hesperetin-Cu (II) complex was investigated. Hesperetin-Cu (II) complex strongly inhibited three stages glycosylation products in bovine serum albumin (BSA)-fructose model, especially for the inhibition of AGEs (88.45%), which was stronger than hesperetin (51.76%) and aminoguanidine (22.89%). Meanwhile, hesperetin-Cu (II) complex decreased the levels of BSA carbonylation and oxidation products. 182.50 µg/mL of hesperetin-Cu (II) complex inhibited 66.71% β-crosslinking structures of BSA, and scavenged 59.80% superoxide anions and 79.76% hydroxyl radicals. Moreover, after incubating with methylglyoxal for 24 h, hesperetin-Cu (II) complex removed 85.70% methylglyoxal. The mechanisms of protein antiglycation by hesperetin-Cu (II) complex may be through protecting structure, trapping methylglyoxal, scavenging free radicals and interacting with BSA. This study may contribute to the development of hesperetin-Cu (II) complex as a functional food additive against protein glycation.
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