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Updated: Jan 15, 2026

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
Published on: April 5, 2022
Characterization and binding site profiling of zinc-chelated peptides from Takifugu rubripes bone with enhanced
Mingzhu Guo1, Lei Huang1, Yang Li1
1College of Food Science and Technology, Hebei Agricultural University, Baoding 071001, China.
Abstract:
To develop a novel and bioavailable zinc supplement, collagen peptides were prepared from Takifugu rubripes bone via enzymatic hydrolysis. The low-molecular-weight fraction (<3 kDa, T1) showed the highest zinc-chelating capacity (294.84 mg/g). The T1-Zn complex exhibited enhanced antioxidant activity, stronger antibacterial efficacy against Escherichia coli than Staphylococcus aureus, and significantly improved zinc bioavailability (20.49 %) under simulated gastrointestinal digestion. Structural analyses revealed significant conformational changes following zinc binding, including increased crystallinity, larger particle size, and enhanced thermal stability, along with a reduction in surface charge. Spectroscopic analyses and amino acid profiling confirmed that Zn2+ primarily interacts with the carboxyl and amino groups of Asp, Glu, and Lys, promoting peptide folding and aggregation. LC-MS/MS identified three potential zinc-binding peptides, and molecular docking further confirmed stable coordination via carboxyl oxygen atoms. These results elucidate the structure-activity relationship of peptide-zinc complexes and highlight the potential of T. rubripes bone-derived peptides as safe, bioavailable, and multifunctional zinc carriers for functional food applications.
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