In order to expand the application range of wheat glutamine-derived peptides， the study prepared wheat glutamine-derived peptides from gluten powder and investigated the temperature， pH， metal ions， and in vitro simulated digestion stability. Wheat glutamine-derived peptide segments were identified using triple quadrupole liquid chromatography tandem mass spectrometry (LC-MS)， and the binding sites and binding capacity of the wheat glutamine-derived peptide segments to the antidepressant target protein brain-derived neurotrophic factor (BDNF) were studied using molecular docking technology， further analyzing the antidepressant activity of the wheat glutamine-derived peptide segments. The results showed that wheat glutamine-derived peptide had good thermal stability， acid-base stability and in vitro digestion stability， and metal Cu2+ had a great influence on its stability. Five wheat glutamine-derived peptides， Leu-Gly-Gln (LGQ)， PyroGlu-Leu-Gln (pELQ)， PyroGlu-Gln-Leu (pEQL)， PyroGlu-Gln-Gln (pEQQ) and Val-Ala-Gln (VAQ)， were identified， and the binding energies of their binding energies to BDNF were -5.03， -6.13， -6.55， -6.03 and -5.18 kcal/mol， respectively. All of them could form stable binders with BDNF and bind to ligands through van der Waals forces， Pi-Alkyl groups and other hydrophobic forces， indicating that these five peptides of wheat glutamine-derived peptide had antidepressant activity. This study provides theoretical support for the production and processing of wheat glutamine-derived peptides and the development of antidepressant nutritional health products.