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Updated: Jul 10, 2025

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
Published on: January 31, 2014
Effects of Covalent or Noncovalent Binding of Different Polyphenols to Acid-Soluble Collagen on Protein Structure,
Yang Wang1, Jiaping Zhou2, Xiaojing Tian1
1Key Laboratory of Food Nutrition and Safety, Ministry of Education, College of Food Science and Engineering, Tianjin University of Science and Technology, Tianjin 300457, China.
Abstract:
In this study, the structure, function, and digestibility of noncovalent complexes and covalent conjugates formed by acid-soluble collagen with polyphenols of different structures (quercetin, epicatechin, gallic acid, chlorogenic acid, procyanidin, and tannic acid) were investigated. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that polyphenols were covalently bound to collagen by laccase catalytic oxidation. Biolayer interferometry revealed that the noncovalent binding strength of polyphenols to collagen from high to low was quercetin > gallic acid > chlorogenic acid > epicatechin, which was consistent with the trend of covalent polyphenol binding. Procyanidin and tannic acid had strong noncovalent binding, but their covalent binding ability was weak. Compared with the pure collagen, the complexes improved emulsification and antioxidant properties (more than 2.5 times), and the conjugates exhibited better thermal stability (99.4-106.8 °C) and antidigestion ability (reduced by more than 37%). The finding sheds new light on the use of collagen as a functional food ingredient in the food industry.
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