ArticleFoods (Basel, Switzerland)2022
Calcium Binding Mechanism of Soybean Peptide with Histidine Alteration by Molecular Docking Analysis and Spectroscopic Methods.
Article in Foods (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- A Comprehensive Review of Kombucha Fermentation and Probiotic Functional Mechanisms: Microbial Dynamics, Bioactive Compounds and Health Effects.Probiotics and antimicrobial proteins · 2026Review
- Therapeutic and immunomodulatory effects of phage therapy in red hybrid tilapia challenged with Klebsiella pneumoniae.Archives of microbiology · 2026Article
- Protective effects of ethanolic lychee (Litchi chinensis Sonn.) seed extract against adipogenesis and inflammation in 3T3-L1 cells.Molecular biology reports · 2025Article
- Evaluating the capability of soybean peptides as calcium ion carriers: a study through sequence analysis and molecular dynamics simulations.RSC advances · 2024Article
- Calcium-binding properties, stability, and osteogenic ability of phosphorylated soy peptide-calcium chelate.Frontiers in nutrition · 2023Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Histidine (His) carries a unique heteroaromatic imidazole side chain and plays an irreplaceable role in peptides and proteins. With the current study, we aimed to determine the characteristics and functional activities of the bone density of soy peptide-calcium complexes in which a His residue was replaced by Leu (CBP-H). Soybean peptide (CBP-H) was chemically synthesized, the binding mechanism between CBP-H and calcium ions in combination was determined with bioinformatics and spectroscopy analysis, and the difference between CBP and CBP-H was investigated. Finally, we analyzed the effect of CBP and CBP-H on osteoblasts in vitro. The results showed that CBP-H could bind to calcium ions, and the calcium coordinated with the carboxyl groups of Asp and Glu in the peptide. The nitrogen atoms of the amino group and the oxygen atoms of the carboxyl group in CBP-H significantly contributed to the coordination with Ca
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