To identify potential α-glucosidase inhibitory peptides within the protein sequence of Larimichthys crocea, the protein was initially simulated to undergo digestion by gastric and intestinal enzymes. Subsequently, 894 peptide sequences were screened and identified through the utilization of various bioinformatics tools, such as Peptideranker, Toxinpred, AllerTop, and Innovagen. Among these sequences, 26 peptides were determined to be non-toxic, non-allergenic, and water-soluble. These peptides were further screened using the AutoDock SailVina software. The outcomes indicated that the binding ability of PPDVPEF, PDF, and PPDY to α-glucosidase surpassed that of the positive control peptide AGGFR. These three peptides could stably bind to the active site of the α-glucosidase receptor and form reliable hydrogen bonds. These results affirm that PPDVPEF, PDF, and PPDY exist in the protein sequence of L. crocea and possess potential α-glucosidase inhibitory activity, thereby providing a theoretical foundation for further research and the preparation of α-glucosidase inhibitory peptides from the L. crocea protein.