Food protein-derived mineral binding peptides for mineral specific carrier design beyond chelation screening

Background Mineral binding by food protein-derived peptides is commonly interpreted as beneficial chelation. However, strong peptide-mineral association may either preserve an accessible mineral pool or immobilize essential minerals in poorly exchangeable complexes. Because apparent binding capacity alone confuses coordination stoichiometry with nutritional significance, mineral accessibility—the capacity to maintain soluble and exchangeable mineral species under realistic conditions—provides a more appropriate evaluation criterion. The central scientific issue is to distinguish peptide carriers from mineral sinks under food-processing and gastrointestinal conditions. Scope and approach This review reorganizes mineral-binding peptide research into a mineral-specific carrier-design framework. Accessibility is operationalized through conditional binding, soluble retention, matrix competition, and epithelial compatibility. Methodological coverage includes INFOGEST digestion with ICP-MS evaluation, EDTA/phytic acid competitive exchange for exchangeability assessment, and Caco-2 monolayer transport combined with bioavailability validation. Small-molecule chelators are used as chemical priors. Enzymatic preparation and fraction standardization are connected with the release of peptide motifs as food-source and ingredient development. AI-guided design is discussed through peptide-ion-condition records that integrate sequence features with mineral identity and assay context. Key findings and conclusions Calcium peptide systems are governed mainly by oxygen-donor motifs and precipitation control. Zinc peptide systems require mixed donor patterns and resistance to phytate displacement. Iron peptide systems require pH-dependent solubility and redox compatibility. Enzymatic production should preserve ion-adapted motifs and generate standardized fractions. AI models require mineral-specific descriptors rather than generic peptide-activity labels. This framework shifts the field from empirical chelation screening toward mechanism-informed, process-compatible mineral-carrier design.