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Formation of Crystalline Nanoparticles by Iron Binding to Pentapeptide (Asp-His-Thr-Lys-Glu) from Egg White Hydrolysates

Abstract

A novel peptide from egg white, Asp-His-Thr-Lys-Glu (DHTKE), contains specific amino acids associated with iron binding. The present study aims to better understand the molecular basis of interactions between the DHTKE peptide and iron ions. The ultraviolet-visible and fluorescence spectra indicate an interaction between the DHTKE peptide and iron ions, which led to the formation of DHTKE-iron complex. Notably, Asp, Glu, His, and Lys in the DHTKE peptide play crucial roles in the formation of DHTKE-iron complex, and the iron-binding site of the DHTKE peptide corresponded primarily to the amide and carboxyl groups. The DHTKE peptide can bind iron ions in a 1:2 ratio with a binding constant as 1.312×105 M-1. Moreover, the DHTKE-iron complex belongs to thermodynamically stable nanoparticles that present in the crystalline structure, which might be attributed to peptide folding induced by iron binding. Meanwhile, the DHTKE-iron complex remains relatively high iron-releasing percentage and exerts excellent solubility in the human gastrointestinal tract in vitro. This suggests a potential application of peptides containing Asp, Glu, His, or Lys residues as potential iron supplements.

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Publication details

The article was received on 09 Jun 2017, accepted on 03 Aug 2017 and first published on 04 Aug 2017


Article type: Paper
DOI: 10.1039/C7FO00843K
Citation: Food Funct., 2017, Accepted Manuscript
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    Formation of Crystalline Nanoparticles by Iron Binding to Pentapeptide (Asp-His-Thr-Lys-Glu) from Egg White Hydrolysates

    N. Sun, P. Cui, D. Li, Z. Jin, S. Zhang and S. Lin, Food Funct., 2017, Accepted Manuscript , DOI: 10.1039/C7FO00843K

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