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Updated: Sep 27, 2025

Protein Kinase C-delta Inhibitor Peptide Formulation using Gold Nanoparticles
Published on: March 9, 2019
Enzymatically synthesized γ-[Glu](n≥1)-Gln as novel calcium-binding peptides to deliver calcium with enhanced
Huan Xiang1, Hui Huang1, Dongxiao Sun-Waterhouse2
1South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences/Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs/National Research and Development Center for Aquatic Product Processing, Guangzhou 510300, Guangdong, China.
Abstract:
Novel γ-[Glu](n≥1)-Gln-Ca chelates were prepared by using γ-[Glu](n≥1)-Gln (mixture peptides containg γ-Glu-Gln, γ-Glu-Glu-Gln, γ-Glu-Glu-Glu-Gln, γ-Glu-Glu-Glu-Glu-Gln, γ-Glu-Glu-Glu-Glu-Glu-Gln) which were synthesized by glutaminase. Based on single factor and orthogonal array experiments, the optimal calcium-chelation conditions were as follows: 30 min chelation at 70 °C; peptide concentration, 0.15 g/mL; mixture peptides-to-calcium mass ratio, 25:1. The particle size of chelates was 743.6 ± 64.2 nm and the chelates appeared stable neutral molecular entities with 91.33% of chelation rate and 35.2 mg/g of calcium, also with higher thermostability. Chelated calcium ions might be surrounded by coordination bonds linking to two or more connecting points: oxygen atoms (carboxyl oxygen, hydroxyl oxygen and oxygen of peptide bonds) and nitrogen atoms (amino nitrogen). The chelates could be used for food/nutraceutical applications, as no toxicity at 0.125-10 mg/mL and enhanced efficiency in calcium release (releasing percentage over 85% at pH 8.0), transport and uptake compared with CaCl2 were detected in Caco-2 cells.
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