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Updated: Aug 16, 2025

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
Published on: January 31, 2014
Preparation of a cattle bone collagen peptide-calcium chelate by the ultrasound method and its structural
Hongru Zhang1,2, Liwei Qi1, Xiaodan Wang3
1Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing, 100193, China. dr_zch@163.com.
Abstract:
This study was designed to prepare a cattle bone-derived collagen peptide-calcium chelate by the ultrasound method (CP-Ca-US), and its structure, stability, and bioactivity on MC3T3-E1 cells were characterized. Single-factor experiments optimized the preparation conditions: ultrasound power 90 W, ultrasound time 40 min, CaCl2/peptides ratio 1/2, pH 7. Under these conditions, the calcium-chelating ability reached 39.48 μg mg-1. The result of Fourier transform-infrared spectroscopy indicated that carboxyl oxygen and amino nitrogen atoms were chelation sites. Morphological analysis indicated that CP-Ca-US was characterized by a porous surface and large particles. Stability analysis demonstrated that CP-Ca-US was stable in the thermal environment and under intestinal digestion. CP-Ca-US showed more stability in gastric juice than the chelate prepared by the hydrothermal method. Cell experiments indicated that CP-Ca-US increased osteoblast proliferation (proliferation rate 153% at a concentration of 300 μg mL-1) and altered the cell cycle. Significantly, CP-Ca-US enhanced calcium absorption by interacting with calcium-sensing receptors and promoted the mineralization of MC3T3-E1 cells. This study provides the scientific basis for applying the ultrasound method to prepare peptide-calcium chelates and clarifies the positive role of chelates in bone building.
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