{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T07:25:36Z","timestamp":1778570736357,"version":"3.51.4"},"reference-count":24,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2024,1,22]],"date-time":"2024-01-22T00:00:00Z","timestamp":1705881600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["scijournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["J Sci Food Agric"],"published-print":{"date-parts":[[2024,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>BACKGROUND<\/jats:title><jats:p>Tyrosinase, a copper\u2010containing metalloenzyme with catalytic activity, is widely found in mammals. It is the key rate\u2010limiting enzyme that catalyzes melanin synthesis. For humans, tyrosinase is beneficial to the darkening of eyes and hair. However, excessive deposition of melanin in the skin can lead to dull skin color and lead to pigmentation. Therefore, many skin\u2010whitening compounds have been developed to decrease tyrosinase activity. This study aimed to identify a new tyrosinase inhibitory peptide through enzymatic hydrolysis, <jats:italic>in vitro<\/jats:italic> activity verification, molecular docking, and molecular dynamics (MD) simulation.<\/jats:p><\/jats:sec><jats:sec><jats:title>RESULTS<\/jats:title><jats:p>A tripeptide Asp\u2010Glu\u2010Arg (DER) was identified, with a \u2018\u2010CDOCKER_Energy\u2019 value of 121.26 Kcal\u2009mol<jats:sup>\u22121<\/jats:sup>. DER has effective tyrosinase inhibitory activity. Research shows that its half maximal inhibitory concentration value is 1.04\u2009\u00b1\u20090.01\u2009mmol\u2009L<jats:sup>\u22121<\/jats:sup>. In addition, DER binds to tyrosinase residues His85, His244, His259, and Asn260, which are key residues that drive the interaction between the peptide and tyrosinase. Finally, through MD simulation, the conformational changes and structural stability of the complexes were further explored to verify and supplement the results of molecular docking.<\/jats:p><\/jats:sec><jats:sec><jats:title>CONCLUSION<\/jats:title><jats:p>This experiment shows that DER can effectively inhibit tyrosinase activity. His244, His259, His260, and Asn260 are the critical residues that drive the interaction between the peptide and tyrosinase, and hydrogen bonding is an important force. DER from <jats:italic>Spirulina<\/jats:italic> has the potential to develop functional products with tyrosinase inhibition. \u00a9 2024 Society of Chemical Industry.<\/jats:p><\/jats:sec>","DOI":"10.1002\/jsfa.13249","type":"journal-article","created":{"date-parts":[[2024,1,15]],"date-time":"2024-01-15T12:33:27Z","timestamp":1705322007000},"page":"3648-3653","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Identification and molecular docking of tyrosinase inhibitory peptides from allophycocyanin in <scp><i>Spirulina platensis<\/i><\/scp>"],"prefix":"10.1002","volume":"104","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9019-5494","authenticated-orcid":false,"given":"Zhipeng","family":"Yu","sequence":"first","affiliation":[{"name":"School of Food Science and Engineering Hainan University  Haikou P. R. China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hong","family":"Lv","sequence":"additional","affiliation":[{"name":"School of Food Science and Engineering Hainan University  Haikou P. R. China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mingjie","family":"Zhou","sequence":"additional","affiliation":[{"name":"School of Food Science and Engineering Bohai University  Jinzhou P. R. China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pengcheng","family":"Fu","sequence":"additional","affiliation":[{"name":"School of Food Science and Engineering Hainan University  Haikou P. R. China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wenzhu","family":"Zhao","sequence":"additional","affiliation":[{"name":"School of Food Science and Engineering Hainan University  Haikou P. R. 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