Antioxidant activity analysis of collagen peptide-magnesium chelate

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 mag-nesium 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 pro-tective and reparative effects against H2O2-induced oxidative damage. This work provides mechanistic insights for further development of peptide-magnesium chelates for oxidative stress mitigation.

Automated summary

This study finds that magnesium can chelate with bovine bone collagen peptides, leading to changes in their structures and functional properties, as well as improving their antioxidant activities and reparative effects against oxidative damage. These findings provide mechanistic insights for the further development of peptide-magnesium chelates for mitigating oxidative stress.