<p>To develop a food-compatible copper delivery system with favorable the digestive stability and potential bioaccessibility of dietary copper while increasing the value of <i>Lanmaoa asiatica</i>, a <i>L. asiatica</i> peptide-copper chelate (LAP-Cu) was prepared and characterized. <i>L. asiatica</i> peptides (LAP) were obtained by enzymatic hydrolysis and separated using gel chromatography, and the fraction with the highest copper-chelating activity showed a chelation rate of 91.40%. SEM-EDS, UV-vis, FT-IR, and XRD analyses indicated that Cu²⁺ was incorporated into the peptide matrix and induced changes in morphology, elemental composition, electronic environment, and molecular arrangement. Spectral changes suggested that amino groups, carboxylate groups, and carbonyl-related groups may participate in Cu²⁺ coordination. During simulated digestion, copper retention decreased during the gastric phase and recovered during the intestinal phase, suggesting digestion-responsive copper retention and possible reassociation under intestinal conditions. Furthermore, Nano-LC-MS/MS identified 863 peptide sequences, from which 18 candidates were selected using a stepwise screening strategy based on molecular weight, metal-coordinating residues, predicted bioactivity, toxicity, solubility, and human intestinal absorption. Molecular docking suggested 9 potential Cu²⁺-binding peptides, with Asp residues frequently involved in the predicted coordination sites. These findings provide a basis for developing mushroom-derived peptide-copper systems for functional food applications and offer preliminary molecular insights into peptide-metal interactions.</p>