Antioxidant activity analysis of collagen peptide-magnesium chelate. (January 2023)

• Record Type: Journal Article
• Authors: Zhang, Chao; Du, Bowei; Song, Zihao; Deng, Guiya; Shi, Yan; Li, Tianyu; Huang, Yaqin
• Is Part Of: Polymer testing. Volume 117(2023)
• Publication Date: 2023-01
• Subjects: Collagen peptides -- Peptide-magnesium chelates -- Antioxidant activity -- Oxidative damage; Polymers -- Testing -- Periodicals; Polymères -- Tests -- Périodiques; 620.1920287
• DOI: 10.1016/j.polymertesting.2022.107822
• Languages: English
• ISSNs: 0142-9418

Abstract

Abstract: Antioxidant peptides from natural polymer collagen are highly desirable and their ability to coordinate with minerals will provide new leads for the prevention and treatment of oxidative stress-related diseases. Here, we tested the changes of structures and functional properties of bovine bone collagen peptides (BBCP) after magnesium chelation. The Fourier transform infrared (FTIR) results revealed that Mg(II) chelated with BBCP mainly via amino nitrogen and carboxyl oxygen atoms. The fluorescence and circular dichroism (CD) results indicated that Mg(II) could induce and stabilize the conformational structures, and change the amino acid distribution on the surfaces of BBCP. The chelation of BBCP and Mg(II) led to the improvement of radical scavenging activities, and enhanced the intracellular antioxidant enzyme activities and GSH levels, thus demonstrating higher protective and reparative effects against H2 O2 -induced oxidative damage. This work provides mechanistic insights for further development of peptide-magnesium chelates for oxidative stress mitigation. Graphical abstract: Image 1 Highlights: Mg 2+ chelates with collagen peptides via amino nitrogen and carboxyl oxygen atoms. Mg 2+ could induce and stabilize the secondary structure of collagen peptides. Magnesium chelation promotes the radical scavenging activity of collagen peptides. Magnesium chelation improves the resistance of mammalian cells to oxidative stress.