Calcium-chelating peptides from rabbit bone collagen: Characterization, identification and mechanism elucidation

This study aimed to characterize and identify calcium-chelating peptides from rabbit bone collagen explore the underlying chelating mechanism. Collagen calcium were extracted by instant ejection steam explosion (ICSE) combined with enzymatic hydrolysis, followed chelation reaction prepare peptide-calcium chelate (RBCP-Ca). The sites further analyzed LC-MS/MS, while mechanism binding modes investigated. structural characterization revealed that RBCP successfully chelated ions. Furthermore, LC-MS/MS analysis indicated included both acidic amino acids (Asp Glu) basic (Lys Arg). Interestingly, three modes, namely Inter-Linking, Loop-Linking Mono-Linking for first time found, Inter-Linking mode accounted highest proportion (75.1%), suggesting of ions frequently occurred between two peptides. Overall, this provides a theoretical basis elucidation