{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T13:09:35Z","timestamp":1791464975559,"version":"4.3.4"},"reference-count":85,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2022,4,22]],"date-time":"2022-04-22T00:00:00Z","timestamp":1650585600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Skin hyperpigmentation resulting from excessive tyrosinase expression has long been a problem for beauty lovers, which has not yet been completely solved. Although researchers are working on finding effective tyrosinase inhibitors, most of them are restricted, due to cell mutation and cytotoxicity. Therefore, functional foods are developing rapidly for their good biocompatibility. Food-derived peptides have been proven to display excellent anti-tyrosinase activity, and the mechanisms involved mainly include inhibition of oxidation, occupation of tyrosinase\u2019s bioactive site and regulation of related gene expression. For anti-oxidation, peptides can interrupt the oxidative reactions catalyzed by tyrosinase or activate an enzyme system, including SOD, CAT, and GSH-Px to scavenge free radicals that stimulate tyrosinase. In addition, researchers predict that peptides probably occupy the site of the substrate by chelating with copper ions or combining with surrounding amino acid residues, ultimately inhibiting the catalytic activity of tyrosinase. More importantly, peptides reduce the tyrosinase expression content, primarily through the cAMP\/PKA\/CREB pathway, with PI3K\/AKT\/GSK3\u03b2, MEK\/ERK\/MITF and p38 MAPK\/CREB\/MITF as side pathways. The objective of this overview is to recap three main mechanisms for peptides to inhibit tyrosinase and the emerging bioinformatic technologies used in developing new inhibitors.<\/jats:p>","DOI":"10.3390\/molecules27092710","type":"journal-article","created":{"date-parts":[[2022,4,23]],"date-time":"2022-04-23T21:39:45Z","timestamp":1650749985000},"page":"2710","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":80,"title":["The Hypopigmentation Mechanism of Tyrosinase Inhibitory Peptides Derived from Food Proteins: An Overview"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4109-0236","authenticated-orcid":false,"given":"Yuqiong","family":"Song","sequence":"first","affiliation":[{"name":"Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China"},{"name":"Co-Innovation Center of Jiangsu Marine Bio-Industry Technology, Jiangsu Ocean University, Lianyungang 222005, China"},{"name":"College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shengjun","family":"Chen","sequence":"additional","affiliation":[{"name":"Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China"},{"name":"Co-Innovation Center of Jiangsu Marine Bio-Industry Technology, Jiangsu Ocean University, Lianyungang 222005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laihao","family":"Li","sequence":"additional","affiliation":[{"name":"Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China"},{"name":"Co-Innovation Center of Jiangsu Marine Bio-Industry Technology, Jiangsu Ocean University, Lianyungang 222005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yaoxun","family":"Zeng","sequence":"additional","affiliation":[{"name":"School of Biomedical and Pharmaceutical Sciences, Guangdong University of Technology, Guangzhou 510006, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiao","family":"Hu","sequence":"additional","affiliation":[{"name":"Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China"},{"name":"Co-Innovation Center of Jiangsu Marine Bio-Industry Technology, Jiangsu Ocean University, Lianyungang 222005, China"},{"name":"Collaborative Innovation Center of Provincial and Ministerial Co-Construction for Marine Food Deep Processing, Dalian Polytechnic University, Dalian 116034, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,4,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"129172","DOI":"10.1016\/j.foodchem.2021.129172","article-title":"Comparing the inhibitory abilities of epigallocatechin-3-gallate and gallocatechin gallate against tyrosinase and their combined effects with kojic acid","volume":"349","author":"Song","year":"2021","journal-title":"Food Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1080\/14756366.2018.1545767","article-title":"A comprehensive review on tyrosinase inhibitors","volume":"34","author":"Zolghadri","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.foodchem.2017.09.054","article-title":"Novel hydroxypyridinone derivatives containing an oxime ether moiety: Synthesis, inhibition on mushroom tyrosinase and application in anti-browning of fresh-cut apples","volume":"242","author":"Shao","year":"2018","journal-title":"Food Chem."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.ijbiomac.2020.05.193","article-title":"Inhibitory effects of four anthraquinones on tyrosinase activity: Insight from spectroscopic analysis and molecular docking","volume":"160","author":"Zeng","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Yap, P.G., and Gan, C.Y. (2021). Multifunctional tyrosinase inhibitor peptides with copper chelating, UV-absorption and antioxidant activities: Kinetic and docking studies. Foods, 10.","DOI":"10.3390\/foods10030675"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"2192","DOI":"10.1016\/j.bmc.2019.04.020","article-title":"Antioxidant, anti-tyrosinase and anti-melanogenic effects of (E)-2,3-diphenylacrylic acid derivatives","volume":"27","author":"Ullah","year":"2019","journal-title":"Bioogram. Med. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"104","DOI":"10.3389\/fphar.2017.00104","article-title":"Antioxidant and anti-tyrosinase activities of phenolic extracts from rape bee pollen and inhibitory melanogenesis by cAMP\/MITF\/TYR pathway in B16 mouse melanoma cells","volume":"8","author":"Sun","year":"2017","journal-title":"Front. Pharmacol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"905","DOI":"10.5713\/ajas.2006.905","article-title":"Study on skin care properties of milk kefir whey","volume":"19","author":"Chen","year":"2006","journal-title":"Asian-Australas. J. Anim. Sci."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1016\/j.bbrc.2020.10.105","article-title":"Isolindleyin exerts anti-melanogenic effects in human epidermal melanocytes via direct binding to tyrosinase","volume":"534","author":"Lee","year":"2021","journal-title":"Biochem. Bioph. Res. Commun."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"5241","DOI":"10.1016\/j.bmc.2010.05.045","article-title":"(\u2212)-N-Formylanonaine from michelia alba as a human tyrosinase inhibitor and antioxidant","volume":"18","author":"Wang","year":"2010","journal-title":"Bioogra. Med. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"112480","DOI":"10.1016\/j.ejmech.2020.112480","article-title":"Kojic acid\u2013natural product conjugates as mushroom tyrosinase inhibitors","volume":"201","author":"Ashooriha","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"4892","DOI":"10.1039\/D0FO00003E","article-title":"Inhibitory mechanism of epicatechin gallate in tyrosinase inhibitory interaction, conformational change and computational simulation","volume":"11","author":"Song","year":"2020","journal-title":"Food Funct."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"113205","DOI":"10.1016\/j.lwt.2022.113205","article-title":"Improving tyrosinase inhibitory activity of grass carp fish scale gelatin hydrolysate by gastrointestinal digestion: Purification, identification and action mechanism","volume":"159","author":"Hu","year":"2020","journal-title":"LWT Food Sci. Technol."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Yap, P.G., and Gan, C.Y. (2020). Chicken egg white\u2014Advancing from food to skin health therapy: Optimization of hydrolysis condition and identification of tyrosinase inhibitor peptides. Foods, 9.","DOI":"10.3390\/foods9091312"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"112331","DOI":"10.1016\/j.indcrop.2020.112331","article-title":"Skin-care functions of peptides prepared from Chinese quince seed protein: Sequences analysis, tyrosinase inhibition and molecular docking study","volume":"148","author":"Deng","year":"2020","journal-title":"Ind. Crop. Prod."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1016\/j.jbiosc.2015.10.010","article-title":"New tyrosinase inhibitory decapeptide: Molecular insights into the role of tyrosine residues","volume":"121","author":"Ochiai","year":"2016","journal-title":"J. Biocci. Bioeng."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.smallrumres.2019.01.015","article-title":"Antioxidant, tyrosinase and urease inhibitory activities of camel \u03b1S-casein and its hydrolysate fractions","volume":"173","author":"Addar","year":"2019","journal-title":"Small Ruminant. Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"129369","DOI":"10.1016\/j.foodchem.2021.129369","article-title":"Understanding the combined effect and inhibition mechanism of 4-hydroxycinnamic acid and ferulic acid as tyrosinase inhibitors","volume":"352","author":"Yu","year":"2021","journal-title":"Food Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1016\/j.csbj.2022.02.007","article-title":"Identification of (Z)-2-benzylidene-dihydroimidazothiazolone derivatives as tyrosinase inhibitors: Anti-melanogenic effects and in silico studies","volume":"20","author":"Choi","year":"2022","journal-title":"Comput. Struct. Biotechnol. J."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"131848","DOI":"10.1016\/j.foodchem.2021.131848","article-title":"Improved yield of theaflavin-3,3\u2019-digallate from bacillus megaterium tyrosinase via directed evolution","volume":"375","author":"Zhou","year":"2022","journal-title":"Food Chem."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Kong, S., Choi, H.R., Kim, Y.J., Lee, Y.S., Park, K.C., and Kwak, S.Y. (2020). Milk protein-derived antioxidant tetrapeptides as potential hypopigmenting agents. Antioxidants, 9.","DOI":"10.3390\/antiox9111106"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.bcab.2018.12.009","article-title":"Purification and functional characterization of a novel tyrosinase (diphenolase) inhibitory peptides prepared from Solunum tuberosum peels protein via enzymatic hydrolysis","volume":"17","author":"Ali","year":"2019","journal-title":"Biocatal. Agric. Biotechnol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"101123","DOI":"10.1016\/j.bcab.2019.101123","article-title":"Purification of a novel monophenolase inhibitory peptides prepared from Vicia faba pods protein via enzymatic hydrolysis","volume":"19","author":"Ali","year":"2019","journal-title":"Biocatal. Agric. Biotechnol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1007\/s10068-017-0186-z","article-title":"Effects of protein hydrolysate from chicken feather meal on tyrosinase activity and melanin formation in B16F10 murine melanoma cells","volume":"26","author":"Pongkai","year":"2017","journal-title":"Food Sci. Biotechnol."},{"key":"ref_25","first-page":"22067","article-title":"Improvement of skin condition on skin moisture and anti-melanogenesis by collagen peptides from milkfish (Chanos chanos) scales","volume":"382","author":"Chen","year":"2018","journal-title":"Mater. Sci. Eng."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.procbio.2019.05.015","article-title":"Static hydrothermal processing and fractionation for production of a collagen peptide with anti-oxidative and anti-aging properties","volume":"83","author":"Park","year":"2019","journal-title":"Process. Biochem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/0014-5793(74)80500-4","article-title":"Purification and properties of tyrosinase inhibitor from mushroom","volume":"49","author":"Madhosingh","year":"1974","journal-title":"FEBS. Lett."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Ferri, M., Graen-Heedfeld, J., Bretz, K., Guillon, F., Michelini, E., Calabretta, M.M., Lamborghini, M., Gruarin, N., Roda, A., and Kraft, A. (2017). Peptide fractions obtained from rice by-products by means of an environment-friendly process show in vitro health-related bioactivities. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0170954"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/j.carbpol.2015.06.046","article-title":"Antitumor and immunomodulatory activities of a water-soluble polysaccharide from Chaenomeles speciosa","volume":"132","author":"Xie","year":"2015","journal-title":"Carbohydr. Polym."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1021\/acs.jnatprod.6b00449","article-title":"Rice bran protein as a potent source of antimelanogenic peptides with tyrosinase inhibitory activity","volume":"79","author":"Ochiai","year":"2016","journal-title":"J. Nat. Prod."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Babini, E., Taneyo-Saa, D.L., Tassoni, A., Ferri, M., Kraft, A., Gran-Heedfeld, J., Bretz, K., Roda, A., Michelini, E., and Calabretta, M.M. (2020). Microbial fermentation of industrial rice-starch byproduct as valuable source of peptide fractions with health-related activity. Microorganisms, 8.","DOI":"10.3390\/microorganisms8070986"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Thaha, A., Wang, B.S., Chang, Y.W., Hsia, S.M., Huang, T.C., Shiau, C.Y., Hwang, D.F., and Chen, T.Y. (2021). Food-derived bioactive peptides with anti-oxidative capacity, xanthine oxidase and tyrosinase inhibitory activity. Processes, 9.","DOI":"10.3390\/pr9050747"},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Zhang, J.B., Zhao, Y.Q., Wang, Y.M., Chi, C.F., and Wang, B. (2019). Eight collagen peptides from hydrolysate fraction of spanish mackerel skins: Isolation, identification, and in vitro antioxidant activity evaluation. Mar. Drugs, 17.","DOI":"10.3390\/md17040224"},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Ito, N., Seki, S., and Ueda, F. (2018). Effects of composite supplement containing collagen peptide and ornithine on skin conditions and plasma IGF-1 levels\u2014A randomized, double-blind, placebo-controlled trial. Mar. Drugs, 16.","DOI":"10.3390\/md16120482"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1007\/s11802-010-0094-9","article-title":"Anti-oxidation activities of low-molecular-weight gelatin hydrolysate isolated from the sea cucumber Stichopus japonicus","volume":"9","author":"Wang","year":"2010","journal-title":"J. Ocean Univ. China."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.foodchem.2017.01.049","article-title":"Influence of hydrolysis behaviour and microfluidisation on the functionality and structural properties of collagen hydrolysates","volume":"227","author":"Zhang","year":"2017","journal-title":"Food Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1016\/j.foodchem.2012.05.113","article-title":"The functional property of egg yolk phosvitin as a melanogenesis inhibitor","volume":"135","author":"Jung","year":"2012","journal-title":"Food Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.peptides.2006.11.023","article-title":"Novel peptides with tyrosinase inhibitory activity","volume":"28","author":"Schurink","year":"2007","journal-title":"Peptides"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1633","DOI":"10.1080\/14756366.2019.1661401","article-title":"Novel tyrosinase inhibitory peptide with free radical scavenging ability","volume":"34","author":"Shen","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"7995","DOI":"10.1038\/srep07995","article-title":"Discovery of highly potent tyrosinase inhibitor, T1, with significant anti-melanogenesis ability by zebrafish in vivo assay and computational molecular modeling","volume":"5","author":"Chen","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.jbiosc.2020.04.002","article-title":"Evaluation of tyrosinase inhibitory activity and mechanism of Leucrocin I and its modified peptides","volume":"130","author":"Joompang","year":"2020","journal-title":"J. Biosci. Bioeng."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"129471","DOI":"10.1016\/j.foodchem.2021.129471","article-title":"Separation, identification, and molecular docking of defatted walnut (Juglans regia L.) meal","volume":"353","author":"Feng","year":"2021","journal-title":"Food Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"e2100204","DOI":"10.1002\/ardp.202100204","article-title":"The C\u2013terminally shortened analogs of a hexapeptide derived from Lingzhi hydrolysate with enhanced tyrosinase-inhibitory activity","volume":"354","author":"Krobthong","year":"2021","journal-title":"Arch. Pharm."},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Hong, G.P., Min, S.G., and Jo, Y.J. (2019). Anti-oxidative and anti-aging activities of porcine by-product collagen hydrolysates produced by commercial proteases: Effect of hydrolysis and ultrafiltration. Molecules, 24.","DOI":"10.3390\/molecules24061104"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1007\/s00726-020-02879-4","article-title":"Identification of chia seed (Salvia hispanica L.) peptides with enzyme inhibition activity towards skin-aging enzymes","volume":"52","author":"Liceaga","year":"2020","journal-title":"Amino Acids."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"113551","DOI":"10.1016\/j.indcrop.2021.113551","article-title":"Skin-protective properties of peptide extracts produced from white sorghum grain kafirins","volume":"167","author":"Rivera","year":"2021","journal-title":"Ind. Crop. Prod."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1080\/10826068.2020.1789991","article-title":"Extraction, anti-tyrosinase, and antioxidant activities of the collagen hydrolysate derived from Rhopilema hispidum","volume":"51","author":"Salim","year":"2021","journal-title":"Prep. Biochem. Biotechnol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1007\/s10695-016-0306-3","article-title":"Zebrafish phosvitin-derived peptide Pt5 inhibits melanogenesis via cAMP pathway","volume":"43","author":"Liu","year":"2017","journal-title":"Fish Physiol. Biochem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"4508","DOI":"10.1016\/j.biomaterials.2014.01.052","article-title":"The transdermal inhibition of melanogenesis by a cell-membrane-permeable peptide delivery system based on poly-arginine","volume":"35","author":"Ookubo","year":"2014","journal-title":"Biomaterials"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2843","DOI":"10.1016\/j.bmcl.2004.03.046","article-title":"Solid-phase synthesis of kojic acid-tripeptides and their tyrosinase inhibitory activity, storage stability, and toxicity","volume":"14","author":"Kim","year":"2004","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.cellsig.2017.09.004","article-title":"Recent development of signaling pathways inhibitors of melanogenesis","volume":"40","author":"Pillaiyar","year":"2017","journal-title":"Cell Signal."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1111\/j.1751-1097.2007.00226.x","article-title":"The protective role of melanin against UV damage in human skin","volume":"84","author":"Brenner","year":"2008","journal-title":"Photochem. Photobiol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/j.tifs.2021.08.017","article-title":"Bioactive peptides derived from marine sources: Biological and functional properties","volume":"119","author":"Cunha","year":"2022","journal-title":"Trends. Food Sci. Tech."},{"key":"ref_54","first-page":"218","article-title":"Recent progress in preventive effect of collagen peptides on photoaging skin and action mechanism","volume":"11","author":"Li","year":"2022","journal-title":"FSHW"},{"key":"ref_55","first-page":"447","article-title":"Skin pigmentation","volume":"49","author":"Lakhan","year":"2021","journal-title":"Pigment. Probl."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1007\/s12010-016-2208-3","article-title":"A novel heptapeptide with tyrosinase inhibitory activity identified from a phage display library","volume":"181","author":"Nie","year":"2020","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"128265","DOI":"10.1016\/j.foodchem.2020.128265","article-title":"Synthesis, antioxidant and anti-tyrosinase activity of 1,2,4-triazole hydrazones as antibrowning agents","volume":"341","author":"Peng","year":"2021","journal-title":"Food Chem."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Hu, Z.Z., Sha, X.M., Zhang, L., Huang, S., and Tu, Z.C. (2022). Effect of grass carp scale collagen peptide FTGML on cAMP-PI3K\/Akt and MAPK signaling pathways in B16F10 melanoma cells and correlation between anti-melanin and antioxidant properties. Foods, 11.","DOI":"10.3390\/foods11030391"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1016\/0304-4165(88)90023-2","article-title":"The role of sulfhydryl compounds in mammalian melanogenesis effect of cysteine and glutathione upon tyrosinase and the intermediates of the pathway","volume":"967","author":"Jara","year":"1988","journal-title":"Biochim. Biophys. Acta."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"111619","DOI":"10.1016\/j.lwt.2021.111619","article-title":"In silico investigation and assessment of plausible novel tyrosinase inhibitory peptides from sesame seeds","volume":"147","author":"Baskaran","year":"2021","journal-title":"LWT Food Sci. Technol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1080\/07391102.2014.893203","article-title":"A new insight into mushroom tyrosinase inhibitors: Docking, pharmacophore-based virtual screening, and molecular modeling studies","volume":"33","author":"Bagherzadeh","year":"2015","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"132283","DOI":"10.1016\/j.molstruc.2021.132283","article-title":"Design, synthesis, biological evaluation, and molecular docking study of thioxo-2,3-dihydroquinazolinone derivative as tyrosinase inhibitors","volume":"125","author":"Sepehri","year":"2022","journal-title":"J. Mol. Struct."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.bioorg.2018.10.026","article-title":"Carbazole and hydrazone derivatives as new competitive inhibitors of tyrosinase: Experimental clues to binuclear copper active site binding","volume":"83","author":"Ghani","year":"2019","journal-title":"Bioorg. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"20190280","DOI":"10.1515\/ijfe-2019-0280","article-title":"Copper-chelating peptide from salmon by-product proteolysate","volume":"16","author":"Vo","year":"2020","journal-title":"Int. J. Food Eng."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"34993","DOI":"10.1038\/srep34993","article-title":"The unravelling of the complex pattern of tyrosinase inhibition","volume":"6","author":"Deri","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"4505","DOI":"10.1038\/ncomms5505","article-title":"Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins","volume":"5","author":"Goldfeder","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"114147","DOI":"10.1016\/j.ejmech.2022.114147","article-title":"Cinnamic acid derivatives linked to arylpiperazines as novel potent inhibitors of tyrosinase activity and melanin synthesis","volume":"231","author":"Romagnoli","year":"2022","journal-title":"Eur. J. Med. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"112072","DOI":"10.1016\/j.mcat.2021.112072","article-title":"Considerations about the kinetic mechanism of tyrosinase in its action on monophenols: A review","volume":"518","year":"2022","journal-title":"Mol. Catal."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1601","DOI":"10.1016\/j.jid.2018.01.019","article-title":"Inhibition of human tyrosinase requires molecular motifs distinctively different from mushroom tyrosinase","volume":"138","author":"Mann","year":"2018","journal-title":"J. Investig. Dermatol."},{"key":"ref_70","unstructured":"(2022, April 19). BIOPEP. Available online: https:\/\/biochemia.uwm.edu.pl\/biopep-uwm\/."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Kongsompong, S., E-kobon, T., and Chumnanpuen, P. (2021). K-nearest neighbor and random forest-based prediction of putative tyrosinase inhibitory peptides of abalone haliotis diversicolor. Molecules, 26.","DOI":"10.3390\/molecules26123671"},{"key":"ref_72","unstructured":"(2022, April 19). HELPDOCK. Available online: http:\/\/huanglab.phys.hust.edu.cn\/hpepdock\/."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/j.jgr.2020.11.003","article-title":"Anti-melanogenic property of ginsenoside Rf from Panax ginseng via inhibition of CREB\/MITF pathway in melanocytes and ex vivo human skin","volume":"45","author":"Lee","year":"2021","journal-title":"J. Ginseng. Res."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1016\/j.steroids.2011.06.008","article-title":"Diethylstilbestrol enhances melanogenesis via cAMP-PKA-mediating up-regulation of tyrosinase and MITF in mouse B16 melanoma cells","volume":"76","author":"Jian","year":"2011","journal-title":"Steroids"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1016\/j.bbrc.2016.06.105","article-title":"Vasoactive intestinal peptide stimulates melanogenesis in B16F10 mouse melanoma cells via CREB\/MITF\/tyrosinase signaling","volume":"477","author":"Yuan","year":"2016","journal-title":"Biochem. Bioph. Res. Commun."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"112651","DOI":"10.1016\/j.biopha.2022.112651","article-title":"Decursin prevents melanogenesis by suppressing MITF expression through the regulation of PKA\/CREB, MAPKs, and PI3K\/Akt\/GSK-3\u03b2 cascades","volume":"147","author":"Choi","year":"2022","journal-title":"Biomed. Pharmacother."},{"key":"ref_77","first-page":"100949","article-title":"\u03b1-Mangostin suppressed melanogenesis in B16F10 murine melanoma cells through GSK3\u03b2 and ERK signaling pathway","volume":"26","author":"Zhou","year":"2021","journal-title":"Biochem. Biophys. Rep."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1271\/bbb.90778","article-title":"Sulforaphane inhibited melanin synthesis by regulating tyrosinase gene expression in B16 mouse melanoma cells","volume":"74","author":"Shirasugi","year":"2020","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"595","DOI":"10.3892\/ijmm.2017.2884","article-title":"The lactoferricin B-derived peptide, LfB17-34, induces melanogenesis in B16F10 cells","volume":"39","author":"Huang","year":"2017","journal-title":"Int. J. Mol. Med."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1318","DOI":"10.1016\/j.procbio.2015.05.007","article-title":"A novel peptide purified from the fermented microalga Pavlova lutheri attenuates oxidative stress and melanogenesis in B16F10 melanoma cells","volume":"50","author":"Oh","year":"2015","journal-title":"Process. Biochem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1034","DOI":"10.1016\/j.bbrc.2020.01.051","article-title":"Dasatinib, a second-generation tyrosine kinase inhibitor, induces melanogenesis via ERK-CREB-MITF-tyrosinase signaling in normal human melanocytes","volume":"523","author":"Kang","year":"2020","journal-title":"Biochem. Bioph. Res. Commun."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.cbi.2016.08.023","article-title":"Dihydromyricetin from Ampelopsis grossedentata inhibits melanogenesis through down-regulation of MAPK, PKA and PKC signaling pathways","volume":"258","author":"Huang","year":"2016","journal-title":"Chem.-Biol. Interact."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/j.jdermsci.2019.03.004","article-title":"Fargesin inhibits melanin synthesis in murine malignant and immortalized melanocytes by regulating PKA\/CREB and P38\/MAPK signaling pathways","volume":"94","author":"Fu","year":"2019","journal-title":"J. Dermatol. Sci."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"2679","DOI":"10.1016\/j.jid.2021.01.040","article-title":"TGF\u03b22 upregulates tyrosinase activity through opsin-3 in human skin melanocytes in vitro","volume":"141","author":"Wang","year":"2021","journal-title":"J. Investig. Dermatol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.jdermsci.2021.05.003","article-title":"A natural compound harmine decreases melanin synthesis through regulation of the DYRK1A\/NFATC3 pathway","volume":"103","author":"Park","year":"2021","journal-title":"J. Dermatol. Sci."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/27\/9\/2710\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T22:59:07Z","timestamp":1760137147000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/27\/9\/2710"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,4,22]]},"references-count":85,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2022,5]]}},"alternative-id":["molecules27092710"],"URL":"https:\/\/doi.org\/10.3390\/molecules27092710","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,4,22]]}}}