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An Exploration of the Calcium-Binding Mode of Egg White Peptide, Asp-His-Thr-Lys-Glu, and In Vitro Calcium Absorption Studies of Peptide–Calcium Complex

文献作者：Na Sun, Ziqi Jin, Dongmei Li, Hongjie Yin, and Songyi Lin   《J. Agric. Food Chem.》

ABSTRACTS

The binding mode between the pentapeptide (DHTKE) from egg white hydrolysates and calcium ions was elucidated upon its structural and thermodynamics characteristics. The present study demonstrated that the DHTKE peptide could spontaneously bind calcium with a 1:1 stoichiometry, and that the calcium-binding site corresponded to the carboxyl oxygen, amino nitrogen, and imidazole nitrogen atoms of the DHTKE peptide. Moreover, the effect of the DHTKE–calcium complex on improving the calcium absorption was investigated in vitro using Caco-2 cells. Results showed that the DHTKE–calcium complex could facilitate the calcium influx into the cytosol and further improve calcium absorption across Caco-2 cell monolayers by more than 7 times when compared to calcium-free control. This study facilitates the understanding about the binding mechanism between peptides and calcium ions as well as suggests a potential application of egg white peptides as nutraceuticals to improve calcium absorption.
KEY WORDS
SCREENSHOT

RELATED PRODUCTS
Asp-His-Thr-Lys-Glu (DHTKE), was synthesized in 98.85% purity by China Peptides Co., Ltd. (Shanghai, China).
CHAINING
https://pubs.acs.org/doi/abs/10.1021/acs.jafc.7b03705
Number of Residues:5
1-Letter Code:DHTKE
3-Letter Code:Asp-His-Thr-Lys-Glu

Molecular weight (Mr):628.64 g/mol
Isoelectric point:5.2
Net charge at pH 7.0:-0.9
Average hydrophilicity:1.6
Ratio of hydrophilic residues / total number of residues:60 %
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