{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,25]],"date-time":"2026-03-25T21:06:04Z","timestamp":1774472764931,"version":"3.50.1"},"reference-count":98,"publisher":"MDPI AG","issue":"18","license":[{"start":{"date-parts":[[2025,9,20]],"date-time":"2025-09-20T00:00:00Z","timestamp":1758326400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Biologically active peptides can be obtained with various research methods, depending on the starting material, biological activity, and intended use. To use the most efficient method, it is worth combining in silico and in vitro experiments. Among the tools that can support an in silico analysis are databases such as the Antimicrobial Peptide Database (AMPD) or BIOPEP-UWM. The aim of this study was to make an in silico hydrolysis of peptides with anticancer properties selected from the AMP database, using pepsin, trypsin, and chymotrypsin. Most peptides obtained had properties inhibiting ACE and dipeptidyl peptidase IV activity. Among the resulting peptides, those with the sequence AR, CF, ER, TF, IY, ER, AW, GF, TW, SK and IM are potentially resistant to peptidase from microbial action. An analysis of the peptides\u2019 characteristics showed that peptides with the sequence AR, EK, ER and SK are well-soluble in water and have high affinity for protein and ligand binding. Peptides with the sequence TF, IL and PF are unstable. Thermostable peptides are PGL, IL, GL, IY, VF, PL, IM and QL. The results of the study may be used to design in vitro experiments.<\/jats:p>","DOI":"10.3390\/ijms26189189","type":"journal-article","created":{"date-parts":[[2025,9,22]],"date-time":"2025-09-22T13:04:44Z","timestamp":1758546284000},"page":"9189","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Plant Antimicrobial Oligopeptides with Anticancer Properties as a Source of Biologically Active Peptides\u2014An In Silico Study"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1087-2000","authenticated-orcid":false,"given":"Anna","family":"Jakubczyk","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Food Chemistry, University of Life Sciences in Lublin, 20-950 Lublin, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2100-1315","authenticated-orcid":false,"given":"Kamila","family":"Rybczy\u0144ska-Tkaczyk","sequence":"additional","affiliation":[{"name":"Department of Environmental Microbiology, University of Life Sciences in Lublin, 20-950 Lublin, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anna","family":"Grenda","sequence":"additional","affiliation":[{"name":"Department of Pneumonology, Oncology and Allergology, Medical University of Lublin, 20-059 Lublin, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2025,9,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Salas, C.E., Badillo-Corona, J.A., Ram\u00edrez-Sotelo, G., and Oliver-Salvador, C. (2015). Biologically Active and Antimicrobial Peptides from Plants. BioMed Res. Int., 2015.","DOI":"10.1155\/2015\/102129"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Sharma, V., Gupta, P., and Sharma, P. (2023). Recent Advancements in Novel Bioactive Peptides and Protein Hydrolysates Isolated from Different Medicinal Plants Along with Their Applications in Food and Pharmaceutical Industries, Springer.","DOI":"10.1007\/s10989-023-10565-8"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"20479","DOI":"10.1021\/acs.jafc.3c06882","article-title":"Plant Protein-Derived Active Peptides: A Comprehensive Review","volume":"71","author":"Zhu","year":"2023","journal-title":"J. Agric. Food Chem."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Mani, S., Bhatt, S.B., Vasudevan, V., Prabhu, D., Rajamanikandan, S., Velusamy, P., Ramasamy, P., and Raman, P. (2022). The Updated Review on Plant Peptides and Their Applications in Human Health, Springer.","DOI":"10.1007\/s10989-022-10437-7"},{"key":"ref_5","first-page":"200\u2013207+215","article-title":"Screening of Antimicrobial Peptides from Plants and Their Application in Food","volume":"40","author":"Liu","year":"2024","journal-title":"Food Mach."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Wu, H., Yu, B., and Cong, H. (2025). Preparation and Applications of Antimicrobial Peptides. Peptide Nano-Chemistry and Nanotechnology: From Molecular Design, Self-Assembly, Biomimetic Synthesis to Applications, Springer.","DOI":"10.1007\/978-981-96-2387-7_12"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"2269","DOI":"10.1007\/s12602-024-10354-9","article-title":"The Roadmap of Plant Antimicrobial Peptides Under Environmental Stress: From Farm to Bedside","volume":"16","author":"Ghanbarzadeh","year":"2024","journal-title":"Probiotics Antimicrob. Proteins"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"953720","DOI":"10.3389\/fmicb.2022.953720","article-title":"Synergistic Antimicrobial Effect of Antimicrobial Peptides CATH-1, CATH-3, and PMAP-36 with Erythromycin Against Bacterial Pathogens","volume":"13","author":"Lu","year":"2022","journal-title":"Front. Microbiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"127822","DOI":"10.1016\/j.micres.2024.127822","article-title":"Antimicrobial Peptides: Opportunities and Challenges in Overcoming Resistance","volume":"286","author":"Bucataru","year":"2024","journal-title":"Microbiol. Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"3825","DOI":"10.1111\/1541-4337.12651","article-title":"Bioactive Peptides from Food Fermentation: A Comprehensive Review of Their Sources, Bioactivities, Applications, and Future Development","volume":"19","author":"Chai","year":"2020","journal-title":"Compr. Rev. Food Sci. Food Saf."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Luo, X., Wu, W., Feng, L., Treves, H., and Ren, M. (2021). Short Peptides Make a Big Difference: The Role of Botany-Derived Amps in Disease Control and Protection of Human Health. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222111363"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.ijbiomac.2022.06.043","article-title":"Plant Antimicrobial Peptides: An Overview about Classification, Toxicity and Clinical Applications","volume":"214","author":"Lima","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Gelinski, J.M.L.N., de Melo Franco, B.D.G., and Fonseca, G.G. (2022). Plant-Derived Antimicrobial Peptides. Antimicrobial Peptides: Challenges and Future Perspectives, Academic Press.","DOI":"10.1016\/B978-0-323-85682-9.00003-9"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Abbas, S.K., Qadeer, S., Khan, M.J., Abbas, S.T., and Shah, N.A. (2024). Plant-Based Peptides: Antibiotics. Recent Advances in Industrial Biochemistry, Springer.","DOI":"10.1007\/978-3-031-50989-6_5"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"5492","DOI":"10.1039\/D3FO01119D","article-title":"Plant Antimicrobial Peptides: A Comprehensive Review of Their Classification, Production, Mode of Action, Functions, Applications, and Challenges","volume":"14","author":"Zou","year":"2023","journal-title":"Food Funct."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"eadt8239","DOI":"10.1126\/sciadv.adt8239","article-title":"A Plant Peptide with Dual Activity against Multidrug-Resistant Bacterial and Fungal Pathogens","volume":"11","author":"Chen","year":"2025","journal-title":"Sci. Adv."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1007\/s10989-017-9643-z","article-title":"Antibacterial Natural Peptide Fractions from Indian Ganoderma Lucidum","volume":"24","author":"Mishra","year":"2018","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"S162","DOI":"10.1080\/10408398.2018.1561418","article-title":"Seeds, Fermented Foods, and Agricultural by-Products as Sources of Plant-Derived Antibacterial Peptides","volume":"59","author":"Chai","year":"2019","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"975","DOI":"10.2174\/0109298665278148231106052509","article-title":"Antiviral Peptides Derived from Plants: Their Designs and Functions","volume":"30","author":"Feyzyab","year":"2023","journal-title":"Protein Pept. Lett."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Feijoo-Coronel, M.L., Mendes, B., Ram\u00edrez, D., Pe\u00f1a-Varas, C., de los Monteros-Silva, N.Q.E., Proa\u00f1o-Bola\u00f1os, C., de Oliveira, L.C., L\u00edvio, D.F., da Silva, J.A., and da Silva, J.M.S.F. (2024). Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic Peptides. Antibiotics, 13.","DOI":"10.3390\/antibiotics13010078"},{"key":"ref_21","first-page":"100860","article-title":"Personalized Medicine: An Alternative for Cancer Treatment","volume":"42","author":"Singh","year":"2024","journal-title":"Cancer Treat. Res. Commun."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1007\/s12032-025-02817-y","article-title":"Precision Oncology: Transforming Cancer Care through Personalized Medicine","volume":"42","author":"Rituraj","year":"2025","journal-title":"Med. Oncol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1186\/s12943-025-02321-x","article-title":"Emerging Artificial Intelligence-Driven Precision Therapies in Tumor Drug Resistance: Recent Advances, Opportunities, and Challenges","volume":"24","author":"Mao","year":"2025","journal-title":"Mol. Cancer"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1038\/s41540-025-00547-5","article-title":"Personalized Cancer Treatment Strategies Incorporating Irreversible and Reversible Drug Resistance Mechanisms","volume":"11","author":"He","year":"2025","journal-title":"npj Syst. Biol. Appl."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.2147\/IJN.S445333","article-title":"Anticancer Mechanisms and Potential Anticancer Applications of Antimicrobial Peptides and Their Nano Agents","volume":"19","author":"Dong","year":"2024","journal-title":"Int. J. Nanomed."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"100121","DOI":"10.1016\/j.crbiot.2023.100121","article-title":"Antimicrobial Peptides with Antiviral and Anticancer Properties and Their Modification and Nanodelivery Systems","volume":"5","author":"Yang","year":"2023","journal-title":"Curr. Res. Biotechnol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1463088","DOI":"10.3389\/fonc.2024.1463088","article-title":"From Defense to Offense: Antimicrobial Peptides as Promising Therapeutics for Cancer","volume":"14","author":"Saberian","year":"2024","journal-title":"Front. Oncol."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Guzm\u00e1n-Rodr\u00edguez, J.J., Ochoa-Zarzosa, A., L\u00f3pez-G\u00f3mez, R., and L\u00f3pez-Meza, J.E. (2015). Plant Antimicrobial Peptides as Potential Anticancer Agents. BioMed Res. Int., 2015.","DOI":"10.1155\/2015\/735087"},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Flores-Alvarez, L.J., Jim\u00e9nez-Alc\u00e1ntar, P., Ochoa-Zarzosa, A., and L\u00f3pez-Meza, J.E. (2023). The Antimicrobial Peptide \u03b3-Thionin from Habanero Chile (Capsicum chinense) Induces Caspase-Independent Apoptosis on Human K562 Chronic Myeloid Leukemia Cells and Regulates Epigenetic Marks. Molecules, 28.","DOI":"10.3390\/molecules28093661"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1071\/CH16589","article-title":"Synthesis and Protein Engineering Applications of Cyclotides","volume":"70","author":"Qu","year":"2017","journal-title":"Aust. J. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"e3246","DOI":"10.1002\/psc.3246","article-title":"Natural and Grafted Cyclotides in Cancer Therapy: An Insight","volume":"26","author":"Mehta","year":"2020","journal-title":"J. Pept. Sci."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1310443","DOI":"10.3389\/fimmu.2024.1310443","article-title":"Bioactive Peptides: An Alternative Therapeutic Approach for Cancer Management","volume":"15","author":"Ghadiri","year":"2024","journal-title":"Front. Immunol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"7697","DOI":"10.1021\/jm800704e","article-title":"Engineering Stabilized Vascular Endothelial Growth Factor-A Antagonists: Synthesis, Structural Characterization, and Bioactivity of Grafted Analogues of Cyclotides","volume":"51","author":"Gunasekera","year":"2008","journal-title":"J. Med. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"12974","DOI":"10.1038\/srep12974","article-title":"Design of Substrate-Based BCR-ABL Kinase Inhibitors Using the Cyclotide Scaffold","volume":"5","author":"Huang","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1002\/psc.2782","article-title":"Cystine-Knot Peptides Targeting Cancer-Relevant Human Cytotoxic T Lymphocyte-Associated Antigen 4 (CTLA-4)","volume":"21","author":"Valldorf","year":"2015","journal-title":"J. Pept. Sci."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1016\/j.chembiol.2015.07.012","article-title":"The Prototypic Cyclotide Kalata B1 Has a Unique Mechanism of Entering Cells","volume":"22","author":"Henriques","year":"2015","journal-title":"Chem. Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"23705","DOI":"10.3390\/ijms151223705","article-title":"Lunasin Sensitivity in Non-Small Cell Lung Cancer Cells Is Linked to Suppression of Integrin Signaling and Changes in Histone Acetylation","volume":"15","author":"Inaba","year":"2014","journal-title":"Int. J. Mol. Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"4649","DOI":"10.18632\/oncotarget.3080","article-title":"The Soybean-Derived Peptide Lunasin Inhibits Non-Small Cell Lung Cancer Cell Proliferation by Suppressing Phosphorylation of the Retinoblastoma Protein","volume":"6","author":"McConnell","year":"2015","journal-title":"Oncotarget"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"25525","DOI":"10.18632\/oncotarget.16066","article-title":"The Soy-Derived Peptide Lunasin Inhibits Invasive Potential of Melanoma Initiating Cells","volume":"8","author":"Shidal","year":"2017","journal-title":"Oncotarget"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1021\/acs.bioconjchem.0c00025","article-title":"Enzyme-Instructed Self-Assembly for Cancer Therapy and Imaging","volume":"31","author":"Kim","year":"2020","journal-title":"Bioconjug. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1124\/mol.116.108084","article-title":"Tumor Microenvironment Targeting and Responsive Peptide-Based Nanoformulations for Improved Tumor Therapy","volume":"92","author":"Qin","year":"2017","journal-title":"Mol. Pharmacol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/j.nantod.2015.09.001","article-title":"Nanoscale Assemblies of Small Molecules Control the Fate of Cells","volume":"10","author":"Shi","year":"2015","journal-title":"Nano Today"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"102718","DOI":"10.1016\/j.copbio.2022.102718","article-title":"Synthetic Molecular Evolution of Antimicrobial Peptides","volume":"75","author":"Chen","year":"2022","journal-title":"Curr. Opin. Biotechnol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1002\/fsn3.1423","article-title":"Novel Dipeptidyl Peptidase-IV and Angiotensin-I-Converting Enzyme Inhibitory Peptides Released from Quinoa Protein by in Silico Proteolysis","volume":"8","author":"Guo","year":"2020","journal-title":"Food Sci. Nutr."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1002\/dvdy.20569","article-title":"Importin \u03b1 MRNAs Have Distinct Expression Profiles during Spermatogenesis","volume":"235","author":"Hogarth","year":"2006","journal-title":"Dev. Dyn."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1038\/s41419-022-05167-z","article-title":"Nuclear Import of PTPN18 Inhibits Breast Cancer Metastasis Mediated by MVP and Importin \u03922","volume":"13","author":"Wang","year":"2022","journal-title":"Cell Death Dis."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.pharmthera.2016.03.020","article-title":"Importins and Exportins as Therapeutic Targets in Cancer","volume":"164","author":"Mahipal","year":"2016","journal-title":"Pharmacol. Ther."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Kao, H.J., Weng, T.H., Chen, C.H., Chen, Y.C., Chi, Y.H., Huang, K.Y., and Weng, S.L. (2024). Integrating In Silico and In Vitro Approaches to Identify Natural Peptides with Selective Cytotoxicity against Cancer Cells. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25136848"},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Radchenko, T., Brink, A., Siegrist, Y., Kochansky, C., Bateman, A., Fontaine, F., Morettoni, L., and Zamora, I. (2017). Software-Aided Approach to Investigate Peptide Structure and Metabolic Susceptibility of Amide Bonds in Peptide Drugs Based on High Resolution Mass Spectrometry. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0186461"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"103486","DOI":"10.1016\/j.jff.2019.103486","article-title":"Elucidation of the Role of in Silico Methodologies in Approaches to Studying Bioactive Peptides Derived from Foods","volume":"61","author":"Iwaniak","year":"2019","journal-title":"J. Funct. Foods"},{"key":"ref_51","first-page":"501","article-title":"Mechanism, Preparation, Evaluation and Related Research Progress of Plant-Derived Antihypertensive Peptides","volume":"43","author":"Zhu","year":"2022","journal-title":"Sci. Technol. Food Ind."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"An\u00f3n, M.C., Quiroga, A., Scilingo, A., and Tironi, V. (2023). Plant Bioactive Peptides: From Oilseed, Legume, Cereal, Fruit, and Vegetable. Handbook of Food Bioactive Ingredients: Properties and Applications, Springer.","DOI":"10.1007\/978-3-031-28109-9_18"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1097\/FJC.0b013e318162011f","article-title":"The Antihypertensive Effects of Quercetin in a Salt-Sensitive Model of Hypertension","volume":"51","author":"Mackraj","year":"2008","journal-title":"J. Cardiovasc. Pharmacol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1007\/s10989-021-10309-6","article-title":"A Mini-Review on Potential of Neuropeptides as Future Therapeutics","volume":"28","author":"Sharma","year":"2022","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Li, X., Zuo, S., Wang, B., Zhang, K., and Wang, Y. (2022). Antimicrobial Mechanisms and Clinical Application Prospects of Antimicrobial Peptides. Molecules, 27.","DOI":"10.3390\/molecules27092675"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"111271","DOI":"10.1016\/j.foodres.2022.111271","article-title":"In Silico Modelling of Protein Digestion: A Case Study on Solid\/Liquid and Blended Meals","volume":"157","author":"Gerrits","year":"2022","journal-title":"Food Res. Int."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"307","DOI":"10.53365\/efood.k\/146945","article-title":"Recent Advance of in Vitro Models in Natural Phytochemicals Absorption and Metabolism","volume":"2","author":"Huang","year":"2021","journal-title":"eFood"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1002\/fft2.186","article-title":"Guidelines for in Vitro Simulated Digestion and Absorption of Food","volume":"4","author":"Xin","year":"2023","journal-title":"Food Front."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"19470","DOI":"10.1021\/acs.jafc.4c04368","article-title":"Discovery, Expression, and In Silico Safety Evaluation of Honey Truffle Sweetener, a Sweet Protein Derived from Mattirolomyces Terfezioides and Produced by Heterologous Expression in Komagataella Phaffii","volume":"72","author":"McFarland","year":"2024","journal-title":"J. Agric. Food Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"105562","DOI":"10.1016\/j.yrtph.2024.105562","article-title":"Comprehensive Safety Assessment of Serendipity Berry Sweet Protein Produced from Komagataella Phaffii","volume":"147","author":"Freeman","year":"2024","journal-title":"Regul. Toxicol. Pharmacol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"661463","DOI":"10.3389\/fnut.2021.661463","article-title":"Protein Concentrates on Tepary Bean (Phaseolus acutifolius Gray) as a Functional Ingredient: In Silico Docking of Tepary Bean Lectin to Peroxisome Proliferator-Activated Receptor Gamma","volume":"8","year":"2021","journal-title":"Front. Nutr."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"106092","DOI":"10.1016\/j.idairyj.2024.106092","article-title":"In Silico and in Vitro Analysis of Dipeptidyl Peptidase-IV and Angiotensin-Converting Enzyme Inhibitory Peptides Derived from Milk Lactoferrin","volume":"160","author":"Elisha","year":"2025","journal-title":"Int. Dairy J."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1292297","DOI":"10.3389\/fsufs.2024.1292297","article-title":"Plant Protein-Derived Peptides: Frontiers in Sustainable Food System and Applications","volume":"8","author":"Nirmal","year":"2024","journal-title":"Front. Sustain. Food Syst."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/j.tifs.2020.09.019","article-title":"Plant Protein-Derived Antioxidant Peptides: Isolation, Identification, Mechanism of Action and Application in Food Systems: A Review","volume":"105","author":"Wen","year":"2020","journal-title":"Trends Food Sci. Technol."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Zhu, Z., Xu, Z., Li, Y., Fan, Y., Zhou, Y., Song, K., and Meng, L. (2024). Antioxidant Function and Application of Plant-Derived Peptides. Antioxidants, 13.","DOI":"10.3390\/antiox13101203"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.tifs.2020.02.012","article-title":"Advances on the Antioxidant Peptides from Edible Plant Sources","volume":"99","author":"Wong","year":"2020","journal-title":"Trends Food Sci. Technol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"e12761","DOI":"10.1111\/jfbc.12761","article-title":"Structural and Functional Properties of Food Protein-derived Antioxidant Peptides","volume":"43","author":"Nwachukwu","year":"2019","journal-title":"J. Food Biochem."},{"key":"ref_68","unstructured":"Aguilar, J.G.S. (2021). Plant-Based Peptides with Biological Properties. Phytopharmaceuticals: Potential Therapeutic Applications, Wiley-Scrivener."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"106751","DOI":"10.1016\/j.jff.2025.106751","article-title":"Exploring the Structure\u2013Activity Relationships and Molecular Mechanisms of Food-Derived Antioxidative Peptides in Mitigating Oxidative Stress: A Comprehensive Review","volume":"127","author":"Ali","year":"2025","journal-title":"J. Funct. Foods"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"756","DOI":"10.3389\/fpls.2019.00756","article-title":"Plant and Microalgae Derived Peptides Are Advantageously Employed as Bioactive Compounds in Cosmetics","volume":"10","author":"Apone","year":"2019","journal-title":"Front. Plant Sci."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"408","DOI":"10.2174\/0929866529666220106100225","article-title":"Current Trends and Applications of Food-Derived Antihypertensive Peptides for the Management of Cardiovascular Disease","volume":"29","author":"Shukla","year":"2022","journal-title":"Protein Pept. Lett."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.jfutfo.2022.03.003","article-title":"Review on Plant-Derived Bioactive Peptides: Biological Activities, Mechanism of Action and Utilizations in Food Development","volume":"2","author":"Fan","year":"2022","journal-title":"J. Futur. Foods"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1080\/87559129.2021.1936005","article-title":"Understanding the Mechanism for the Structure-Activity Relationship of Food-Derived ACEI Peptides","volume":"39","author":"Ding","year":"2023","journal-title":"Food Rev. Int."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1007\/s12010-019-03124-9","article-title":"Evaluation of Anti-Inflammatory Efficacy of RA-V: A Natural Cyclopeptide","volume":"190","author":"Rupachandra","year":"2020","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Liu, W., Chen, X., Li, H., Zhang, J., An, J., and Liu, X. (2022). Anti-Inflammatory Function of Plant-Derived Bioactive Peptides: A Review. Foods, 11.","DOI":"10.3390\/foods11152361"},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Malhotra, R., Rana, N., Manwatkar, S., and Kumar, B. (2024). Application of Peptides for the Treatment of Diabetes: A Plant-Based Bioactive Material. Biosystems, Biomedical & Drug Delivery Systems Characterization, Restoration and Optimization, Springer.","DOI":"10.1007\/978-981-97-2596-0_15"},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"de Medeiros, A.F., de Queiroz, J.L.C., Maciel, B.L.L., and de Ara\u00fajo Morais, A.H. (2022). Hydrolyzed Proteins and Vegetable Peptides: Anti-Inflammatory Mechanisms in Obesity and Potential Therapeutic Targets. Nutrients, 14.","DOI":"10.3390\/nu14030690"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"101860","DOI":"10.1016\/j.fbio.2022.101860","article-title":"Differential Effects of Oilseed Protein Hydrolysates in Attenuating Inflammation in Murine Macrophages","volume":"49","author":"Han","year":"2022","journal-title":"Food Biosci."},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Barragan-Galvez, J.C., Gonzalez-Rivera, M.L., Jim\u00e9nez-Cruz, J.C., Hernandez-Flores, A., de la Rosa, G., Lopez-Moreno, M.L., Ya\u00f1ez-Barrientos, E., Romero-Hern\u00e1ndez, M., Deveze-Alvarez, M.A., and Navarro-Santos, P. (2024). A Patent-Pending Ointment Containing Extracts of Five Different Plants Showed Antinociceptive and Anti-Inflammatory Mechanisms in Preclinical Studies. Pharmaceutics, 16.","DOI":"10.3390\/pharmaceutics16091215"},{"key":"ref_80","first-page":"52","article-title":"Anti-Inflammatory Medicinal Plants and the Molecular Mechanisms Underlying Their Activities","volume":"12","author":"Nworu","year":"2015","journal-title":"Afr. J. Tradit. Complement. Altern. Med."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1146\/annurev-nutr-061121-094344","article-title":"Intestinal Amino Acid Transport and Metabolic Health","volume":"43","year":"2023","journal-title":"Annu. Rev. Nutr."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1007\/s13668-022-00401-8","article-title":"Plant-Based Diet: Is It as Good as an Animal-Based Diet When It Comes to Protein?","volume":"11","author":"Ewy","year":"2022","journal-title":"Curr. Nutr. Rep."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"2008S","DOI":"10.1093\/jn\/138.10.2008S","article-title":"The Metabolism of Proline as Microenvironmental Stress Substrate","volume":"138","author":"Phang","year":"2008","journal-title":"J. Nutr."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"420","DOI":"10.4306\/pi.2016.13.4.420","article-title":"Decreased Prolidase Activity in Patients with Posttraumatic Stress Disorder","volume":"13","author":"Demir","year":"2016","journal-title":"Psychiatry Investig."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1111\/cts.12985","article-title":"Estimating Peptide Half-Life in Serum from Tunable, Sequence-Related Physicochemical Properties","volume":"14","author":"Cavaco","year":"2021","journal-title":"Clin. Transl. Sci."},{"key":"ref_86","doi-asserted-by":"crossref","unstructured":"Mathur, D., Singh, S., Mehta, A., Agrawal, P., and Raghava, G.P.S. (2018). In Silico Approaches for Predicting the Half-Life of Natural and Modified Peptides in Blood. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0196829"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"114322","DOI":"10.1016\/j.addr.2022.114322","article-title":"Characterization and Impact of Peptide Physicochemical Properties on Oral and Subcutaneous Delivery","volume":"186","author":"Klepach","year":"2022","journal-title":"Adv. Drug Deliv. Rev."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"5781","DOI":"10.1021\/acsomega.9b03848","article-title":"Peptide Combination Generator: A Tool for Generating Peptide Combinations","volume":"5","author":"Ali","year":"2020","journal-title":"ACS Omega"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"144968","DOI":"10.1016\/j.foodchem.2025.144968","article-title":"Potential Antidiabetic Activity and Permeability Assessment of the Modified Yeast-Derived Peptide, VLSTSFPPW (VW9)","volume":"490","author":"Alahyaribeik","year":"2025","journal-title":"Food Chem."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1046\/j.1365-2796.2003.01228.x","article-title":"Antibacterial Peptides: Basic Facts and Emerging Concepts","volume":"254","author":"Boman","year":"2003","journal-title":"J. Intern. Med."},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Qutb, A.M., Wei, F., and Dong, W. (2020). Prediction and Characterization of Cationic Arginine-Rich Plant Antimicrobial Peptide SM-985 From Teosinte (Zea Mays ssp. Mexicana). Front. Microbiol., 11.","DOI":"10.3389\/fmicb.2020.01353"},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Decker, A.P., Mechesso, A.F., and Wang, G. (2022). Expanding the Landscape of Amino Acid-Rich Antimicrobial Peptides: Definition, Deployment in Nature, Implications for Peptide Design and Therapeutic Potential. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms232112874"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"2210387","DOI":"10.1002\/adfm.202210387","article-title":"Design of Stimuli-Responsive Peptides and Proteins","volume":"33","author":"Li","year":"2023","journal-title":"Adv. Funct. Mater."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1038\/s41538-021-00109-z","article-title":"Rational Design of Hyperstable Antibacterial Peptides for Food Preservation","volume":"5","author":"Vishweshwaraiah","year":"2021","journal-title":"npj Sci. Food"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"100053","DOI":"10.1016\/j.fochms.2021.100053","article-title":"Peptides Derived from the Gastrointestinal Digestion of Amaranth 11S Globulin: Structure and Antioxidant Functionality","volume":"3","author":"Nardo","year":"2021","journal-title":"Food Chem. Mol. Sci."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1548603","DOI":"10.3389\/fmed.2025.1548603","article-title":"Cationic Antimicrobial Peptides: Potential Templates for Anticancer Agents","volume":"12","year":"2025","journal-title":"Front. Med."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"104206","DOI":"10.1016\/j.drudis.2024.104206","article-title":"Peptides as Innovative Strategies to Combat Drug Resistance in Cancer Therapy","volume":"29","author":"Lamb","year":"2024","journal-title":"Drug Discov. Today"},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Minkiewicz, P., Iwaniak, A., and Darewicz, M. (2019). BIOPEP-UWM Database of Bioactive Peptides: Current Opportunities. Int. J. Mol. 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