{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T09:02:17Z","timestamp":1781686937838,"version":"3.54.5"},"reference-count":147,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2026,6,15]],"date-time":"2026-06-15T00:00:00Z","timestamp":1781481600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmaceutics"],"abstract":"<jats:p>Dipeptidyl peptidase-4 (DPP-4) is an established therapeutic target in the treatment of type 2 diabetes mellitus (T2DM), primarily due to its role in regulating incretin activity and glucose homeostasis. Although clinically approved DPP-4 inhibitors are widely used, their moderate efficacy has driven the search for novel compounds with improved properties. In this context, natural products have attracted considerable attention as a source of structurally diverse and biologically active molecules. At the same time, molecular docking has emerged as a key computational tool for the identification and evaluation of potential DPP-4 inhibitors. This review summarizes and critically analyzes current molecular docking studies of natural compounds targeting DPP-4. Over 150 studies were evaluated with respect to docking methodologies, selection of protein structures, and validation strategies. The results reveal substantial variability in computational protocols. Frequently used protein structures include ligand-bound DPP-4 models such as 1X70 and 6B1E. Among the investigated compounds, flavonoids represent the most extensively studied class, followed by alkaloids, phenolics, terpenoids, and peptides. Despite numerous reports of favorable binding interactions within the DPP-4 active site, many studies rely solely on docking results without further validation. The limited use of molecular dynamics simulations and experimental assays highlights a significant gap in the current literature. Overall, while molecular docking provides valuable preliminary insights, improved standardization and integration with complementary approaches are essential to enhance the reliability and translational relevance of in silico findings.<\/jats:p>","DOI":"10.3390\/pharmaceutics18060741","type":"journal-article","created":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T08:22:56Z","timestamp":1781684576000},"page":"741","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Molecular Docking of Natural Compounds as DPP-4 Inhibitors in Type 2 Diabetes: A Comprehensive Review"],"prefix":"10.3390","volume":"18","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-4418-7762","authenticated-orcid":false,"given":"Justyna","family":"Baranowska","sequence":"first","affiliation":[{"name":"Department of Organic and Physical Chemistry, Faculty of Pharmacy, Medical University of Warsaw, Banacha 1 Str., 02-093 Warsaw, Poland"},{"name":"Chair and Department of Pharmaceutical Biology, Medical University of Warsaw, Banacha 1, 02-097 Warsaw, Poland"},{"name":"Doctoral School, Medical University of Warsaw, \u017bwirki i Wigury 81 Str., 02-093 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8258-2849","authenticated-orcid":false,"given":"Anna","family":"Kiss","sequence":"additional","affiliation":[{"name":"Chair and Department of Pharmaceutical Biology, Medical University of Warsaw, Banacha 1, 02-097 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5302-3797","authenticated-orcid":false,"given":"\u0141ukasz","family":"Szeleszczuk","sequence":"additional","affiliation":[{"name":"Department of Organic and Physical Chemistry, Faculty of Pharmacy, Medical University of Warsaw, Banacha 1 Str., 02-093 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,6,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/S0140-6736(23)01301-6","article-title":"Global, Regional, and National Burden of Diabetes from 1990 to 2021, with Projections of Prevalence to 2050: A Systematic Analysis for the Global Burden of Disease Study 2021","volume":"402","author":"Ong","year":"2023","journal-title":"Lancet"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1016\/j.mcna.2004.04.013","article-title":"Pathogenesis of Type 2 Diabetes Mellitus","volume":"88","author":"DeFronzo","year":"2004","journal-title":"Med. Clin. N. Am."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1038\/s41574-020-0399-8","article-title":"Dipeptidyl Peptidase 4 Inhibitors in the Treatment of Type 2 Diabetes Mellitus","volume":"16","author":"Deacon","year":"2020","journal-title":"Nat. Rev. Endocrinol."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Mathur, V., Alam, O., Siddiqui, N., Jha, M., Manaithiya, A., Bawa, S., Sharma, N., Alshehri, S., Alam, P., and Shakeel, F. (2023). Insight into Structure Activity Relationship of DPP-4 Inhibitors for Development of Antidiabetic Agents. Molecules, 28.","DOI":"10.3390\/molecules28155860"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"103810","DOI":"10.1016\/j.bioorg.2020.103810","article-title":"Drug Discovery Approaches Targeting the Incretin Pathway","volume":"99","author":"Deng","year":"2020","journal-title":"Bioorg. Chem."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Nojima, H., Kanou, K., Terashi, G., Takeda-Shitaka, M., Inoue, G., Atsuda, K., Itoh, C., Iguchi, C., and Matsubara, H. (2016). Comprehensive Analysis of the Co-Structures of Dipeptidyl Peptidase IV and Its Inhibitor. BMC Struct. Biol., 16.","DOI":"10.1186\/s12900-016-0062-8"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1016\/j.ejmech.2018.04.061","article-title":"Current Anti-Diabetic Agents and Their Molecular Targets: A Review","volume":"152","author":"Kerru","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.bbrc.2013.03.010","article-title":"A Comparative Study of the Binding Modes of Recently Launched Dipeptidyl Peptidase IV Inhibitors in the Active Site","volume":"434","author":"Nabeno","year":"2013","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"13384","DOI":"10.3390\/molecules200713384","article-title":"Molecular Docking and Structure-Based Drug Design Strategies","volume":"20","author":"Ferreira","year":"2015","journal-title":"Molecules"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1007\/s12551-016-0247-1","article-title":"Software for Molecular Docking: A Review","volume":"9","author":"Pagadala","year":"2017","journal-title":"Biophys. Rev."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1016\/j.neuron.2018.08.011","article-title":"Molecular Dynamics Simulation for All","volume":"99","author":"Hollingsworth","year":"2018","journal-title":"Neuron"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Salmaso, V., and Moro, S. (2018). Bridging Molecular Docking to Molecular Dynamics in Exploring Ligand-Protein Recognition Process: An Overview. Front. Pharmacol., 9.","DOI":"10.3389\/fphar.2018.00923"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1080\/14756360802610761","article-title":"Inhibition of Dipeptidyl Peptidase IV (DPP IV) Is One of the Mechanisms Explaining the Hypoglycemic Effect of Berberine","volume":"24","author":"Mohammad","year":"2009","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.phymed.2012.09.009","article-title":"Antihyperglycemic Activity with DPP-IV Inhibition of Alkaloids from Seed Extract of Castanospermum Australe: Investigation by Experimental Validation and Molecular Docking","volume":"20","author":"Bharti","year":"2012","journal-title":"Phytomedicine"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/j.phymed.2016.03.004","article-title":"Effect of Glycosin Alkaloid from Rhizophora Apiculata in Non-Insulin Dependent Diabetic Rats and Its Mechanism of Action: In Vivo and in Silico Studies","volume":"23","author":"Selvaraj","year":"2016","journal-title":"Phytomedicine"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"e2983","DOI":"10.1002\/jmr.2983","article-title":"Purification, Biochemical Characterization, and DPP-IV and \u03b1-Amylase Inhibitory Activity of Berberine from Cardiospermum halicacabum","volume":"35","author":"Naik","year":"2022","journal-title":"J. Mol. Recognit."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"3443","DOI":"10.2147\/DDDT.S454091","article-title":"Isolation and Quantification of Palmatine from Fibraurea tinctoria Lour: In Vitro Antioxidant Activity and In Silico Antidiabetic Activity Evaluation","volume":"18","author":"Purwaningsih","year":"2024","journal-title":"Drug Des. Devel. Ther."},{"key":"ref_18","first-page":"230","article-title":"Tetrahydrobisbenzylisoquinoline Alkaloids from Phaeanthus ophthalmicus Inhibit Target Enzymes Associated with Type 2 Diabetes and Obesity","volume":"14","author":"Manzano","year":"2024","journal-title":"J. Appl. Pharm. Sci."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"37","DOI":"10.33263\/BRIAC153.037","article-title":"Antioxidant Capacity, Inhibitor of Alpha-Glucosidase and DPP-IV of Kesambi (Schleichera oleosa) Leaf Extract and Their Compound Profiles Based on LC-ESI-MS Analysis: In Vitro and In Silico Study","volume":"15","author":"Nursamsiar","year":"2025","journal-title":"Biointerface Res. Appl. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"65","DOI":"10.33263\/BRIAC155.065","article-title":"In Silico Screening and Molecular Docking Studies of Unique Phytoconstituents Present in Different Unripe Fruits as Potential Antidiabetic and Anti-Hyperlipidemic Agents","volume":"15","author":"Giri","year":"2025","journal-title":"Biointerface Res. Appl. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"062013","DOI":"10.1088\/1757-899X\/546\/6\/062013","article-title":"Alkaloid Fraction of Litsea Glutinosa Leaves Provides an Important Precursor for Inhibition of Dipeptidyl Peptidase 4 Activity","volume":"546","author":"Kisnawaty","year":"2019","journal-title":"IOP Conf. Ser. Mater. Sci. Eng."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Macalalad, M.A.B., and Gonzales, A.A. (2023). In Silico Screening and Identification of Antidiabetic Inhibitors Sourced from Phytochemicals of Philippine Plants against Four Protein Targets of Diabetes (PTP1B, DPP-4, SGLT-2, and FBPase). Molecules, 28.","DOI":"10.3390\/molecules28145301"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"6145","DOI":"10.1080\/07391102.2022.2103029","article-title":"DPP-4 Inhibition Mediated Antidiabetic Potential of Phytoconstituents of an Aqueous Fruit Extract of Withania coagulans (Stocks) Dunal: In-Silico, in-Vitro and in-Vivo Assessments","volume":"41","author":"Kumar","year":"2023","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Zhao, Z., Ma, R., Ma, Y., Zhao, L., Wang, L., Fang, Y., Zhang, Y., Wu, X., and Wang, X. (2024). Discovery of Nine Dipeptidyl Peptidase-4 Inhibitors from Coptis Chinensis Using Virtual Screening, Bioactivity Evaluation, and Binding Studies. Molecules, 29.","DOI":"10.3390\/molecules29102304"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"4064","DOI":"10.1111\/ijfs.17163","article-title":"Antidiabetic Potential of Ethanolic Crude Extract of Garcinia Atroviridis Fruits: In Vitro, in Ovo, and in Silico Analysis","volume":"59","author":"Shahid","year":"2024","journal-title":"Int. J. Food Sci. Technol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"24936","DOI":"10.1038\/s41598-024-75570-3","article-title":"GC\u2013MS Analysis, Molecular Docking, and Pharmacokinetic Studies on Dalbergia Sissoo Barks Extracts for Compounds with Anti-Diabetic Potential","volume":"14","author":"Vijh","year":"2024","journal-title":"Sci. Rep."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"100354","DOI":"10.1016\/j.kjs.2024.100354","article-title":"In Vitro and in Silico Synergistic Antidiabetic Effectiveness of Several Multi-Drug Combinations of Siraitia grosvenorii, Dimocarpus longan Lour., and Orthosiphon stamineus Benth. Extracts","volume":"52","author":"Zhao","year":"2025","journal-title":"Kuwait J. Sci."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Singh, A.K., Patel, P.K., Choudhary, K., Joshi, J., Yadav, D., and Jin, J.O. (2020). Quercetin and Coumarin Inhibit Dipeptidyl Peptidase-IV and Exhibits Antioxidant Properties: In Silico, in Vitro, Ex Vivo. Biomolecules, 10.","DOI":"10.3390\/biom10020207"},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Ahmad, I., Arifianti, A.E., Sakti, A.S., Saputri, F.C., and Mun\u2019im, A. (2020). Simultaneous Natural Deep Eutectic Solvent-Based Ultrasonic-Assisted Extraction of Bioactive Compounds of Cinnamon Bark and Sappan Wood as a Dipeptidyl Peptidase IV Inhibitor. Molecules, 25.","DOI":"10.3390\/molecules25173832"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.52711\/0974-360X.2022.00180","article-title":"Non-Targeted Screening with LC-HRMS and In-Silico Study on Diabetic Activity of Ethyl Acetate Extract of Sanrego (Lunasia Amara Blanco)","volume":"15","author":"Adriani","year":"2022","journal-title":"Res. J. Pharm. Technol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1016\/j.freeradbiomed.2025.10.251","article-title":"Cichoriin, a Coumarin Glycoside with Antidiabetic Effect and Cardioprotective Activity against H2O2 induced Oxidative Stress in H9c2 Cells: In-Vitro and in-Silico Study","volume":"241","author":"Sishu","year":"2025","journal-title":"Free Radic. Biol. Med."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1833","DOI":"10.1007\/s11696-023-03209-0","article-title":"Computational Screening of Phytocompound Isolated from the Plant Toddalia asiatica and Coleonema album as Potential Inhibitors against Enzyme DPP-4 as a Treatment for Type-2 Diabetes Mellitus","volume":"78","author":"Upendra","year":"2024","journal-title":"Chem. Pap."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.diabres.2012.02.011","article-title":"DPP-IV Inhibitory Potential of Naringin: An in Silico, in Vitro and in Vivo Study","volume":"97","author":"Parmar","year":"2012","journal-title":"Diabetes Res. Clin. Pract."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"479505","DOI":"10.1155\/2013\/479505","article-title":"Berry and Citrus Phenolic Compounds Inhibit Dipeptidyl Peptidase IV: Implications in Diabetes Management","volume":"2013","author":"Fan","year":"2013","journal-title":"Evid.-Based Complement. Altern. Med."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/j.apjtb.2015.05.014","article-title":"Anti-Diabetic Potential of Urena Lobata Leaf Extract through Inhibition of Dipeptidyl Peptidase IV Activity","volume":"5","author":"Purnomo","year":"2015","journal-title":"Asian Pac. J. Trop. Biomed."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1186\/s40200-017-0328-0","article-title":"Active Phytochemicals of Pueraria Tuberosa for DPP-IV Inhibition: In Silico and Experimental Approach","volume":"16","author":"Srivastava","year":"2017","journal-title":"J. Diabetes Metab. Disord."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Kim, B.R., Kim, H.Y., Choi, I., Kim, J.B., Jin, C.H., and Han, A.R. (2018). DPP-IV Inhibitory Potentials of Flavonol Glycosides Isolated from the Seeds of Lens Culinaris: In Vitro and Molecular Docking Analyses. Molecules, 23.","DOI":"10.3390\/molecules23081998"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"12141","DOI":"10.1021\/acs.jafc.0c04974","article-title":"Effects of Different Dietary Flavonoids on Dipeptidyl Peptidase-IV Activity and Expression: Insights into Structure-Activity Relationship","volume":"68","author":"Gao","year":"2020","journal-title":"J. Agric. Food Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"102042","DOI":"10.1016\/j.bcab.2021.102042","article-title":"Structure Based Virtual Screening of Natural Compounds and Molecular Dynamics Simulation: Butirosin as Dipeptidyl Peptidase (DPP-IV) Inhibitor","volume":"35","author":"Paul","year":"2021","journal-title":"Biocatal. Agric. Biotechnol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1177\/15593258221093275","article-title":"Biochemical Investigation of Inhibitory Activities of Plant-Derived Bioactive Compounds Against Carbohydrate and Glucagon-Like Peptide-1 Metabolizing Enzymes","volume":"20","author":"Khalid","year":"2022","journal-title":"Dose Response"},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Bouslamti, M., Loukili, E.H., Elrherabi, A., El Moussaoui, A., Chebaibi, M., Bencheikh, N., Nafidi, H.A., Bin Jardan, Y.A., Bourhia, M., and Bnouham, M. (2023). Phenolic Profile, Inhibition of \u03b1-Amylase and \u03b1-Glucosidase Enzymes, and Antioxidant Properties of Solanum elaeagnifolium Cav. (Solanaceae): In Vitro and In Silico Investigations. Processes, 11.","DOI":"10.3390\/pr11051384"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1007\/s40200-023-01249-7","article-title":"Cheminformatics Identification of Modulators of Key Carbohydrate-Metabolizing Enzymes from C. cujete for Type-2 Diabetes Mellitus Intervention","volume":"22","author":"Balogun","year":"2023","journal-title":"J. Diabetes Metab. Disord."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"235","DOI":"10.52756\/ijerr.2024.v40spl.020","article-title":"Antidiabetic Potency of Flavonoids Using a Systematic Computer-Aided Drug Design Platform","volume":"40","author":"Rath","year":"2024","journal-title":"Int. J. Exp. Res. Rev."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"101092","DOI":"10.1016\/j.fochx.2023.101092","article-title":"The Profiles of Free, Esterified and Insoluble-Bound Phenolics in Peach Juice after High Pressure Homogenization and Evaluation of Their Antioxidant Capacities, Cytoprotective Effect, and Inhibitory Effects on \u03b1-Glucosidase and Dipeptidyl Peptidase-IV","volume":"21","author":"Bie","year":"2024","journal-title":"Food Chem. X"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Ali, M., Hassan, M., Ansari, S.A., Alkahtani, H.M., Al-Rasheed, L.S., and Ansari, S.A. (2024). Quercetin and Kaempferol as Multi-Targeting Antidiabetic Agents against Mouse Model of Chemically Induced Type 2 Diabetes. Pharmaceuticals, 17.","DOI":"10.3390\/ph17060757"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.5530\/ijper.58.4.140","article-title":"HR-LCMS Metabolite Profiling and in Silico Evaluation of the Antidiabetic Activity of Methanolic Leaf Extract of Chrozophora rottleri (Geiseler) A. Juss. Ex Spreng","volume":"58","author":"Nallapaty","year":"2024","journal-title":"Indian J. Pharm. Educ. Res."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"3426","DOI":"10.1080\/14786419.2024.2337108","article-title":"Antidiabetic Effectiveness of Phyllanthus niruri Bioactive Compounds via Targeting DPP-IV","volume":"39","author":"Bhushan","year":"2025","journal-title":"Nat. Prod. Res."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2397","DOI":"10.5530\/ctbp.2025.3.25","article-title":"In-Silico Estimation of Flavonoids through Molecular Docking and Assessment of ADMET Properties as DPP-IV Inhibitor in the Treatment of Diabetes Mellitus","volume":"19","author":"Anas","year":"2025","journal-title":"Curr. Trends Biotechnol. Pharm."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"e202403368","DOI":"10.1002\/cbdv.202403368","article-title":"Computational Evaluation of Phytocompounds From Selective Medicinal Plants as Potential Antidiabetic Agents","volume":"22","author":"Kumar","year":"2025","journal-title":"Chem. Biodivers."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Ojo, O.A., Ogunlakin, A.D., Ajayi-Odoko, O.A., Gyebi, G.A., Ayokunle, D.I.K., Olanrewaju, A.A., Agbeye, O.D., Ogunwale, E.T., and Adeyemi, O.S. (2025). Bioprospection of Indigenous Herbal Formulations for Diabetes Care: In Vitro, Network Pharmacology, and Molecular Dynamics Studies. BMC Complement. Med. Ther., 25.","DOI":"10.1186\/s12906-025-04980-1"},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Kalhotra, P., Chittepu, V.C.S.R., Osorio-Revilla, G., and Gallardo-Vel\u00e1zquez, T. (2018). Structure\u2013Activity Relationship and Molecular Docking of Natural Product Library Reveal Chrysin as a Novel Dipeptidyl Peptidase-4 (DPP-4) Inhibitor: An Integrated in Silico and in Vitro Study. Molecules, 23.","DOI":"10.3390\/molecules23061368"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.bbrc.2018.04.156","article-title":"Citrus Bioflavonoids Dipeptidyl Peptidase-4 Inhibition Compared with Gliptin Antidiabetic Medications","volume":"503","author":"Gupta","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1007\/s13205-018-1138-x","article-title":"Flavonoid-Rich Extract of Chromolaena odorata Modulate Circulating GLP-1 in Wistar Rats: Computational Evaluation of TGR5 Involvement","volume":"8","author":"Omotuyi","year":"2018","journal-title":"3 Biotech"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"3192","DOI":"10.4066\/biomedicalresearch.29-18-922","article-title":"Delineating Antidiabetic Proficiency of Catechin from Withania somnifera and Its Inhibitory Action on Dipeptidyl Peptidase-4 (Dpp-4)","volume":"29","author":"Kempegowda","year":"2018","journal-title":"Biomed. Res."},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Kalhotra, P., Chittepu, V.C.S.R., Osorio-Revilla, G., and Gallardo-Vel\u00e1zquez, T. (2019). Discovery of Galangin as a Potential DPP-4 Inhibitor That Improves Insulin-Stimulated Skeletal Muscle Glucose Uptake: A Combinational Therapy for Diabetes. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20051228"},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Quek, A., Kassim, N.K., Ismail, A., Latif, M.A.M., Shaari, K., Tan, D.C., and Lim, P.C. (2021). Identification of Dipeptidyl Peptidase-4 and \u03b1-Amylase Inhibitors from Melicope glabra (Blume) T. G. Hartley (Rutaceae) Using Liquid Chromatography Tandem Mass Spectrometry, In Vitro and In Silico Methods. Molecules, 26.","DOI":"10.3390\/molecules26010001"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"202","DOI":"10.11113\/mjfas.v17n2.2059","article-title":"Molecular Docking of Polyphenol Compounds from Anacardium occidentale with Alpha-Glucosidase and Dipeptidyl-Peptidase-4 Enzymes","volume":"17","author":"Haron","year":"2021","journal-title":"Malays. J. Fundam. Appl. Sci."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Pan, J., Zhang, Q., Zhang, C., Yang, W., Liu, H., Lv, Z., Liu, J., and Jiao, Z. (2022). Inhibition of Dipeptidyl Peptidase-4 by Flavonoids: Structure\u2013Activity Relationship, Kinetics and Interaction Mechanism. Front. Nutr., 9.","DOI":"10.3389\/fnut.2022.892426"},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Afolabi, O.B., Olasehinde, O.R., Olanipon, D.G., Mabayoje, S.O., Familua, O.M., Jaiyesimi, K.F., Agboola, E.K., Idowu, T.O., Obafemi, O.T., and Olaoye, O.A. (2023). Antioxidant Evaluation and Computational Prediction of Prospective Drug-like Compounds from Polyphenolic-Rich Extract of Hibiscus cannabinus L. Seed as Antidiabetic and Neuroprotective Targets: Assessment through in Vitro and in Silico Studies. BMC Complement. Med. Ther., 23.","DOI":"10.1186\/s12906-023-04023-7"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"757","DOI":"10.62110\/sciencein.jist.2024.v12.757","article-title":"Evaluation of O-Methyl Substituted Quercetin Analogues as DPP-4 Inhibitor: In Silico Study","volume":"12","author":"Kamboj","year":"2024","journal-title":"J. Integr. Sci. Technol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"735","DOI":"10.56499\/jppres23.1891_12.4.735","article-title":"In Silico Studies of Ruellia tuberosa L. Compounds as Aldose Reductase, Dipeptidyl Peptidase 4, and \u03b1-Glucosidase Inhibitors against Type 2 Diabetes Mellitus | Estudios in Silico de Compuestos de Ruellia tuberosa L. Como Inhibidores de La Aldosa Reductasa, Dipeptidil Peptidasa 4 y \u03b1-Glucosidasa Contra La Diabetes Mellitus de Tipo 2","volume":"12","author":"Retnaningtyas","year":"2024","journal-title":"J. Pharm. Pharmacogn. Res."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Hossain, A., Rahman, M.E., Faruqe, M.O., Saif, A., Suhi, S., Zaman, R., Hirad, A.H., Matin, M.N., Rabbee, M.F., and Baek, K.H. (2024). Characterization of Plant-Derived Natural Inhibitors of Dipeptidyl Peptidase-4 as Potential Antidiabetic Agents: A Computational Study. Pharmaceutics, 16.","DOI":"10.3390\/pharmaceutics16040483"},{"key":"ref_63","first-page":"90","article-title":"Dipeptidyl Peptidase-4 Inhibition of Peronema canescens Jack Leaves and Stems: Bioassay-Guided Fractionation, Compound Profiling by LC-MS\/MS, and Interaction Mechanism","volume":"14","author":"Elya","year":"2024","journal-title":"J. Appl. Pharm. Sci."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1566","DOI":"10.1080\/07391102.2025.2499671","article-title":"Catechins Anti-Diabetic Actions Are Mediated via Multiple Receptors, a Mechanism Deduced via Molecular Docking and Dynamic Simulations","volume":"44","author":"Salih","year":"2025","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_65","first-page":"75","article-title":"In-Silico Discovery of Dipeptidyl Peptidase-4 Inhibitors from African Medicinal Plants: Molecular Docking, ADMET, Dynamics Simulation, and MM-GBSA Analyses","volume":"69","author":"Akinwumi","year":"2025","journal-title":"Nucl. India"},{"key":"ref_66","first-page":"4621","article-title":"Molecular Docking Study of Standardized Lime (Citrus aurantiifolia) Peel Decoction as an Antidiabetic Herbal","volume":"9","author":"Desmiaty","year":"2025","journal-title":"Trop. J. Nat. Product. Res."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"18292","DOI":"10.1039\/D4RA08509D","article-title":"Antidiabetic Potential of Abelmoschus esculentus Leaves and Fruits: A Comparative Study Assisted by Chemical Profiling, in Vitro and in Silico Studies","volume":"15","author":"Elwekeel","year":"2025","journal-title":"RSC Adv."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"103632","DOI":"10.1016\/j.bcab.2025.103632","article-title":"Enzyme-Assisted Recovery of Phenolic Compounds from Broccoli Waste with Antioxidant and Antihyperglycemic Activities Evaluated through in Vitro and Molecular Docking Studies","volume":"67","year":"2025","journal-title":"Biocatal. Agric. Biotechnol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.plefa.2017.10.004","article-title":"Coconut Phytocompounds Inhibits Polyol Pathway Enzymes: Implication in Prevention of Microvascular Diabetic Complications","volume":"127","author":"Sheela","year":"2017","journal-title":"Prostaglandins Leukot. Essent. Fat. Acids"},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Lammi, C., Bartolomei, M., Bollati, C., Cecchi, L., Bellumori, M., Sabato, E., Vistoli, G., Mulinacci, N., and Arnoldi, A. (2021). Phenolic Extracts from Extra Virgin Olive Oils Inhibit Dipeptidyl Peptidase Iv Activity: In Vitro, Cellular, and in Silico Molecular Modeling Investigations. Antioxidants, 10.","DOI":"10.3390\/antiox10071133"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"103200","DOI":"10.1016\/j.jcs.2021.103200","article-title":"A Comparative Evaluation of in Vitro Antihyperglycemic Potential of Bamboo Seed Rice (Bambusa arundinacea) and Garudan Samba (Oryza sativa): An Integrated Metabolomics, Enzymatic and Molecular Docking Approach","volume":"99","author":"Haldipur","year":"2021","journal-title":"J. Cereal Sci."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1007\/s11418-021-01490-5","article-title":"Anti-Insulin Resistance Effect of Constituents from Senna siamea on Zebrafish Model, Its Molecular Docking, and Structure\u2013Activity Relationships","volume":"75","author":"Nuankaew","year":"2021","journal-title":"J. Nat. Med."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1016\/j.jaim.2021.08.008","article-title":"Dipeptidyl Peptidase-IV Inhibitory Action of Calebin A: An in Silico and in Vitro Analysis","volume":"12","author":"Chalichem","year":"2021","journal-title":"J. Ayurveda Integr. Med."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"110","DOI":"10.22159\/ijap.2022.v14s5.22","article-title":"Antidiabetic Activity of Novel Chromene Compound Isolated from Peperomia pellucida L. Kunth and In Silico Study Against DPP-IV, Alpha-Glucosidase, Alpha-Amylase, and Aldose Reductase for Blood Glucose Homeostasis","volume":"14","author":"Susilawati","year":"2022","journal-title":"Int. J. Appl. Pharm."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.1021\/acs.jafc.4c08713","article-title":"New Hydrogenated Phenanthrene Glycosides from the Edible Vegetable Elatostema tenuicaudatum W.T.Wang with DPP-IV Inhibitory and Hepatoprotective Activity","volume":"73","author":"Hsu","year":"2025","journal-title":"J. Agric. Food Chem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"e202402738","DOI":"10.1002\/cbdv.202402738","article-title":"ADME, Toxicity, Molecular Docking, Molecular Dynamics, Glucokinase Activation, DPP-IV, \u03b1-Amylase, and \u03b1-Glucosidase Inhibition Assays of Mangiferin and Friedelin for Antidiabetic Potential","volume":"22","author":"Suryawanshi","year":"2025","journal-title":"Chem. Biodivers."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"152463","DOI":"10.1016\/j.bbrc.2025.152463","article-title":"Sennoside A from Cassia Angustifolia as a Mixed-Type Inhibitor of DPP-IV: Integrative in Vitro, in Silico, and Kinetic Characterization","volume":"781","author":"Chhabria","year":"2025","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"15585","DOI":"10.1038\/s41598-019-52088-7","article-title":"Natural Phenolic Compounds Potentiate Hypoglycemia via Inhibition of Dipeptidyl Peptidase IV","volume":"9","author":"Huang","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"47","DOI":"10.53879\/id.56.11.11780","article-title":"Amelioration in Insulin Resistance and \u03b2-Cell Function by DPP-4 Inhibition Potential of Trigonella foenum Seed Extract in Type-2 Diabetic Rats","volume":"56","author":"Ram","year":"2019","journal-title":"Indian Drugs"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"196","DOI":"10.4103\/japtr.JAPTR_255_20","article-title":"Molecular Docking Studies of \u03b1-Mangostin, \u03b3-Mangostin, and Xanthone on Peroxisome Proliferator-Activated Receptor Gamma Diphenyl Peptidase-4 Enzyme, and Aldose Reductase Enzyme as an Antidiabetic Drug Candidate","volume":"12","author":"Mahmudah","year":"2021","journal-title":"J. Adv. Pharm. Technol. Res."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"111865","DOI":"10.1016\/j.biopha.2021.111865","article-title":"Syringaldehyde Promoting Intestinal Motility with Suppressing \u03b1-Amylase Hinders Starch Digestion in Diabetic Mice","volume":"141","author":"Weng","year":"2021","journal-title":"Biomed. Pharmacother."},{"key":"ref_82","first-page":"393","article-title":"LIGNAN MATAIRESINOL ILLUSTRATES AN ANTIDIABETIC EFFECT VIA INHIBITION OF DPP-4 AND HEPATO-PROTECTIVE EFFECT VIA INHIBITION OF APOPTOSIS IN DIABETIC RATS","volume":"79","author":"Yang","year":"2022","journal-title":"Acta Pol. Pharm. Drug Res."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"e13686","DOI":"10.1111\/jfbc.13686","article-title":"Identification of Curcumin as a Potential \u03b1-Glucosidase and Dipeptidyl-Peptidase 4 Inhibitor: Molecular Docking Study, in Vitro and in Vivo Biological Evaluation","volume":"46","author":"Cao","year":"2022","journal-title":"J. Food Biochem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"150867","DOI":"10.1016\/j.bbrc.2024.150867","article-title":"Emodin Derivatives as Novel Potent DPP-4 Inhibitors: Design, Synthesis, and in Vitro Evaluation","volume":"735","author":"Masyita","year":"2024","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"30","DOI":"10.20884\/1.jm.2025.20.1.10942","article-title":"Docking Study of Naphthalene Compounds from Eleutherine bulbosa as Antidiabetic Agents on Multiple Receptors","volume":"20","author":"Anam","year":"2025","journal-title":"Molekul"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1093\/jpp\/rgaa038","article-title":"Steroidal Saponins from Trillium govanianum as \u03b1-Amylase, \u03b1-Glucosidase, and Dipeptidyl Peptidase IV Inhibitory Agents","volume":"73","author":"Suresh","year":"2021","journal-title":"J. Pharm. Pharmacol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"274","DOI":"10.25258\/ijddt.14.1.39","article-title":"Network Pharmacology and Molecular Docking Technology-Based Strategy to Explore the Potential Mechanism of Diabecon Formulation Botanicals","volume":"14","author":"Sable","year":"2024","journal-title":"Int. J. Drug Deliv. Technol."},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Kalhotra, P., Chittepu, V.C.S.R., Osorio-Revilla, G., and Gallardo-Velazquez, T. (2020). Phytochemicals in Garlic Extract Inhibit Therapeutic Enzyme DPP-4 and Induce Skeletal Muscle Cell Proliferation: A Possible Mechanism of Action to Benefit the Treatment of Diabetes Mellitus. Biomolecules, 10.","DOI":"10.3390\/biom10020305"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"8016","DOI":"10.1002\/slct.202101661","article-title":"Exploring the Hypoglycaemic Mechanism of Chinese Medicine Xiao-Ke-An Based on Target Dipeptidyl Peptidase 4 Using Molecular Docking and Dynamics Simulation","volume":"6","author":"Yan","year":"2021","journal-title":"ChemistrySelect"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"207","DOI":"10.3889\/oamjms.2022.8356","article-title":"DPP-IV Inhibitory Activity of the Ethanolic Extract of Red Gedi Leaves Abelmoschus manihot L. Medic","volume":"10","author":"Tangka","year":"2022","journal-title":"Open Access Maced. J. Med. Sci."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"20","DOI":"10.31788\/RJC.2022.1516646","article-title":"MOLECULAR DOCKING OF B-SITOSTEROL AND STIGMASTEROL ISOLATED FROM Morinda Citrifolia WITH \u03b1-AMYLASE, \u03b1-GLUCOSIDASE, DIPEPTIDYLPEPTIDASE-IV, AND PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR-\u03b3","volume":"15","author":"Lolok","year":"2022","journal-title":"Rasayan J. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1021\/acsfoodscitech.3c00102","article-title":"In Silico Molecular Docking and Dynamic Investigations of Bioactive Phytoconstituents from Fenugreek Seeds as a Potent Drug against DPP-IV Enzyme","volume":"3","author":"Sarker","year":"2023","journal-title":"ACS Food Sci. Technol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1016\/j.dsx.2020.07.019","article-title":"Phytosterol Supplements Do Not Inhibit Dipeptidyl Peptidase-4","volume":"14","author":"Gupta","year":"2020","journal-title":"Diabetes Metab. Syndr. Clin. Res. Rev."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1735","DOI":"10.26538\/tjnpr\/v5i10.7","article-title":"Molecular Docking of Soybean (Glycine max) Seed and Ginger (Zingiber officinale) Rhizome Components as Anti-Diabetic Through Inhibition of Dipeptidyl Peptidase 4 (DPP-4) and Alpha-Glucosidase Enzymes","volume":"5","author":"Purnomo","year":"2021","journal-title":"Trop. J. Nat. Product. Res."},{"key":"ref_95","first-page":"194","article-title":"Essential Oil of Cymbopogon Citratus against Diabetes: Validation by In Vivo Experiments and Computational Studies","volume":"5","author":"Bharti","year":"2013","journal-title":"J. Bioanal. Biomed."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"134045","DOI":"10.1007\/s11696-024-03754-2","article-title":"Antidiabetic Activity of the Extracted Oil from an Indian Indigenous Plant, Amberboa ramosa: Evidences from in Silico, in Vitro and Enzyme Inhibition Kinetic Studies","volume":"79","author":"Paul","year":"2025","journal-title":"Chem. Pap."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"103","DOI":"10.26538\/tjnpr\/v2i2.9","article-title":"Predicting Binding between Main Molecules of Iranian Oliveria Decumbens and DPP-4 Enzyme Using Molecular Docking","volume":"2","author":"Bouchentouf","year":"2018","journal-title":"Trop. J. Nat. Product. Res."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.cpan.2025.03.002","article-title":"Computational Investigation of Plectranthus Neochilus Essential Oil Phytochemicals Interaction with Dipeptidyl Peptidase 4: A Potential Avenue for Antidiabetic Drug Discovery","volume":"21","author":"Mamoudou","year":"2025","journal-title":"Curr. Pharm. Anal."},{"key":"ref_99","first-page":"18","article-title":"Study of Interaction between Dipeptidyl Peptidase-4 and Products Extracted from the Stevia Plant by Molecular Modeling","volume":"23","author":"Ayachi","year":"2013","journal-title":"Int. J. Pharm. Sci. Rev. Res."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"6147","DOI":"10.1021\/jf500639f","article-title":"Bioactive Compounds from Culinary Herbs Inhibit a Molecular Target for Type 2 Diabetes Management, Dipeptidyl Peptidase IV","volume":"62","author":"Bower","year":"2014","journal-title":"J. Agric. Food Chem."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.phymed.2018.09.195","article-title":"Dipeptidyl Peptidase IV Inhibitory Activity of Terminalia arjuna Attributes to Its Cardioprotective Effects in Experimental Diabetes: In Silico, in Vitro and in Vivo Analyses","volume":"57","author":"Mohanty","year":"2019","journal-title":"Phytomedicine"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"e13807","DOI":"10.1111\/jfbc.13807","article-title":"Effect of Thymoquinone on High Fat Diet and STZ-Induced Experimental Type 2 Diabetes: A Mechanistic Insight by in Vivo and in Silico Studies","volume":"45","author":"Alshahrani","year":"2021","journal-title":"J. Food Biochem."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"27351","DOI":"10.1021\/acsomega.1c04230","article-title":"Antidiabetic Activity of Ficusonolide, a Triterpene Lactone from Ficus foveolata (Wall. Ex Miq.): In Vitro, in Vivo, and in Silico Approaches","volume":"6","author":"Din","year":"2021","journal-title":"ACS Omega"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"95","DOI":"10.3897\/rrpharmacology.8.76237","article-title":"Validation of Structural-Based Virtual Screening Protocols with the PDB Code 3G0B and Prediction of the Activity of Tinospora Crispa Compounds as Inhibitors of Dipeptidyl-Peptidase-IV","volume":"8","author":"Prasetiyo","year":"2022","journal-title":"Res. Results Pharmacol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"112669","DOI":"10.1016\/j.biopha.2022.112669","article-title":"Anti-Diabetic Potential of \u03b2-Boswellic Acid and 11-Keto-\u03b2-Boswellic Acid: Mechanistic Insights from Computational and Biochemical Approaches","volume":"147","author":"Khan","year":"2022","journal-title":"Biomed. Pharmacother."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"207","DOI":"10.4103\/japtr.japtr_376_22","article-title":"Dipeptidyl Peptidase IV Inhibition of Phytocompounds from Artocarpus champeden (Lour.) Stokes: In Silico Molecular Docking Study and ADME-Tox Prediction Approach","volume":"13","author":"Supandi","year":"2022","journal-title":"J. Adv. Pharm. Technol. Res."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"100618","DOI":"10.1016\/j.jaim.2022.100618","article-title":"Antidiabetic and Antihyperlipidemic Effects of Crude Fractions and Isolated Compound from Striga Orobanchioides Benth on Streptozotocin Induced Diabetic Rats","volume":"13","author":"Vikhe","year":"2022","journal-title":"J. Ayurveda Integr. Med."},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Ojo, O.A., Ogunlakin, A.D., Gyebi, G.A., Ayokunle, D.I.K., Odugbemi, A.I., Babatunde, D.E., Ajayi-Odoko, O.A., Iyobhebhe, M., Ezea, S.C., and Akintayo, C.O. (2023). GC-MS Chemical Profiling, Antioxidant, Anti-Diabetic, and Anti-Inflammatory Activities of Ethyl Acetate Fraction of Spilanthes filicaulis (Schumach. and Thonn.) C.D. Adams Leaves: Experimental and Computational Studies. Front. Pharmacol., 14.","DOI":"10.3389\/fphar.2023.1235810"},{"key":"ref_109","first-page":"376","article-title":"Evaluation of Terpenoids as Dipeptidyl Peptidase 4 Lead Molecules: Molecular Docking and Dynamics Simulation Study","volume":"13","author":"Khan","year":"2023","journal-title":"Biointerface Res. Appl. Chem."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"e23289","DOI":"10.1016\/j.heliyon.2023.e23289","article-title":"Inhibitory Effects of Selected Cannabinoids against Dipeptidyl Peptidase IV, an Enzyme Linked to Type 2 Diabetes","volume":"10","author":"Mkabayi","year":"2024","journal-title":"Heliyon"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/j.pathophys.2018.05.003","article-title":"Potential Use of Bitter Melon (Momordica charantia) Derived Compounds as Antidiabetics: In Silico and in Vivo Studies","volume":"25","author":"Elekofehinti","year":"2018","journal-title":"Pathophysiology"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"631","DOI":"10.5958\/0974-360X.2020.00120.1","article-title":"In Silico and in Vitro Screening of Ethanolic Extract of Fruits of Withania Coagulans against Diabetes","volume":"13","author":"Meeran","year":"2020","journal-title":"Res. J. Pharm. Technol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1186\/s12986-021-00547-2","article-title":"Improvements in HOMA Indices and Pancreatic Endocrinal Tissues in Type 2-Diabetic Rats by DPP-4 Inhibition and Antioxidant Potential of an Ethanol Fruit Extract of Withania coagulans","volume":"18","author":"Ram","year":"2021","journal-title":"Nutr. Metab."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"102138","DOI":"10.1016\/j.bcab.2021.102138","article-title":"A Triterpene Glochidon from Phyllanthus debilis: Isolation, Computational Studies, and Antidiabetic Activity Evaluation","volume":"36","author":"Verma","year":"2021","journal-title":"Biocatal. Agric. Biotechnol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"100720","DOI":"10.1016\/j.imu.2021.100720","article-title":"Elucidating the Interactions of Compounds Identified from Aframomum melegueta Seeds as Promising Candidates for the Management of Diabetes Mellitus: A Computational Approach","volume":"26","author":"Ojo","year":"2021","journal-title":"Inform. Med. Unlocked"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1128","DOI":"10.1080\/07391102.2020.1822917","article-title":"Molecular Dynamics Simulation and Free Energy Calculation Studies of Coagulin L as Dipeptidyl Peptidase-4 Inhibitor","volume":"40","author":"Singh","year":"2022","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"10543","DOI":"10.1080\/07391102.2021.1944910","article-title":"In Silico Identification of Antidiabetic Target for Phytochemicals of A. Marmelos and Mechanistic Insights by Molecular Dynamics Simulations","volume":"40","author":"Sharma","year":"2022","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"571","DOI":"10.56499\/jppres22.1345.10.4.571","article-title":"In Silico ADME-T and Molecular Docking Study of Phytoconstituents from Tithonia diversifolia (Hemsl.) A. Gray on Various Targets of Diabetic Nephropathy | ADME-T in Silico y Estudio de Acoplamiento Molecular de Fitoconstituyentes de Tithonia diversifolia (Hemsl.) A. Gray En Varias Dianas de Nefropat\u00eda Diab\u00e9tica","volume":"10","author":"Adianingsih","year":"2022","journal-title":"J. Pharm. Pharmacogn. Res."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"e202401407","DOI":"10.1002\/cbdv.202401407","article-title":"Isospongian Diterpenoids from the Leaves of Amomum Tsao-Ko Promote GLP-1 Secretion via Ca2+\/CaMKII and PKA Pathways and Inhibit DPP-4 Enzyme","volume":"21","author":"Wang","year":"2024","journal-title":"Chem. Biodivers."},{"key":"ref_120","first-page":"615","article-title":"Dipeptidyl-Peptidase-4 Inhibitors from Tinospora Crispa as Revealed By Metabolomics Study, Molecular Docking And Molecular Dynamics Simulation Approaches|Metabolomi \u00c7ali\u015fmalari, Molek\u00fcler Dokunma Ve Molek\u00fcler Dinamik Sim\u00fclasyon Yakla\u015fimlariyla Ortaya \u00c7ikan Tinospora Crispa\u2019dan Dipeptidil-Peptidaz-4 Inhibit\u00f6rleri","volume":"49","author":"Prasetiyo","year":"2025","journal-title":"Ank. Univ. Eczaci. Fak. Derg."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1039\/C5FO01204J","article-title":"Optimization of Enzymatic Production of Anti-Diabetic Peptides from Black Bean (Phaseolus vulgaris L.) Proteins, Their Characterization and Biological Potential","volume":"7","author":"Mojica","year":"2016","journal-title":"Food Funct."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"9601","DOI":"10.1021\/acs.jafc.6b04041","article-title":"Peptides Derived from Soy and Lupin Protein as Dipeptidyl-Peptidase IV Inhibitors: In Vitro Biochemical Screening and in Silico Molecular Modeling Study","volume":"64","author":"Lammi","year":"2016","journal-title":"J. Agric. Food Chem."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"129062","DOI":"10.1016\/j.foodchem.2021.129062","article-title":"Separation, Identification and Molecular Binding Mechanism of Dipeptidyl Peptidase IV Inhibitory Peptides Derived from Walnut (Juglans regia L.) Protein","volume":"347","author":"Kong","year":"2021","journal-title":"Food Chem."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"3798","DOI":"10.1021\/acs.jproteome.1c00081","article-title":"Evaluating Peptides of Picrorhiza Kurroa and Their Inhibitory Potential against ACE, DPP-IV, and Oxidative Stress","volume":"20","author":"Thakur","year":"2021","journal-title":"J. Proteome Res."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"11664","DOI":"10.1080\/07391102.2021.1961868","article-title":"In Silico Study to Predict Potential Precursors of Human Dipeptidyl Peptidase-IV Inhibitors from Hazelnut","volume":"40","author":"Li","year":"2022","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"2010","DOI":"10.1021\/acs.jafc.1c04484","article-title":"Analysis of the Structure and Activity of Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Oligopeptides from Sorghum Kafirin","volume":"70","author":"Dai","year":"2022","journal-title":"J. Agric. Food Chem."},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Wang, W., Liu, X., Li, Y., You, H., Yu, Z., Wang, L., Liu, X., and Ding, L. (2022). Identification and Characterization of Dipeptidyl Peptidase-IV Inhibitory Peptides from Oat Proteins. Foods, 11.","DOI":"10.3390\/foods11101406"},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Rodr\u00edguez-Arana, N., Jim\u00e9nez-Aliaga, K., Intiquilla, A., Le\u00f3n, J.A., Flores, E., Zavaleta, A.I., Izaguirre, V., Solis-Calero, C., and Hern\u00e1ndez-Ledesma, B. (2022). Protection against Oxidative Stress and Metabolic Alterations by Synthetic Peptides Derived from Erythrina Edulis Seed Protein. Antioxidants, 11.","DOI":"10.3390\/antiox11112101"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"8211","DOI":"10.1021\/acs.jafc.3c00603","article-title":"Identification of Novel Dipeptidyl Peptidase-IV Inhibitory Peptides in Chickpea Protein Hydrolysates","volume":"71","author":"Zan","year":"2023","journal-title":"J. Agric. Food Chem."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"9164","DOI":"10.1021\/acs.jafc.3c00535","article-title":"Mining and Validation of Novel Hemp Seed-Derived DPP-IV-Inhibiting Peptides Using a Combination of Multi-Omics and Molecular Docking","volume":"71","author":"Chen","year":"2023","journal-title":"J. Agric. Food Chem."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"4386","DOI":"10.1111\/ijfs.16544","article-title":"Evaluation of the Antihypertensive and Antidiabetic Potential of Peptides from the Globulin Fraction of Quinoa (Chenopodium quinoa) by an in Silico and in Vitro Approach","volume":"58","author":"Chirinos","year":"2023","journal-title":"Int. J. Food Sci. Technol."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Mora-Melgem, J.A., Ar\u00e1mburo-G\u00e1lvez, J.G., C\u00e1rdenas-Torres, F.I., Gonzalez-Santamaria, J., Ram\u00edrez-Torres, G.I., Arvizu-Flores, A.A., Figueroa-Salcido, O.G., and Ontiveros, N. (2023). Dipeptidyl Peptidase IV Inhibitory Peptides from Chickpea Proteins (Cicer arietinum L.): Pharmacokinetics, Molecular Interactions, and Multi-Bioactivities. Pharmaceuticals, 16.","DOI":"10.3390\/ph16081109"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"5193","DOI":"10.1111\/ijfs.16618","article-title":"In Vitro and in Silico Studies of Antioxidant Peptides from Tarwi (Lupinus mutabilis) as Inhibitors of Angiotensin-Converting Enzyme and Dipeptidyl Peptidase IV Enzyme","volume":"58","author":"Chirinos","year":"2023","journal-title":"Int. J. Food Sci. Technol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"14575","DOI":"10.1021\/acs.jafc.3c02733","article-title":"DPP-IV Inhibitory Peptides from Coix Seed Prolamins: Release, Identification, and Analysis of the Interaction between Key Residues and Enzyme Domains","volume":"71","author":"Zhang","year":"2023","journal-title":"J. Agric. Food Chem."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"115521","DOI":"10.1016\/j.lwt.2023.115521","article-title":"Structure-Activity Relationship of Walnut Peptide in Gastrointestinal Digestion, Absorption and Antioxidant Activity","volume":"189","author":"Li","year":"2023","journal-title":"LWT"},{"key":"ref_136","first-page":"e-20230126","article-title":"Antihypertensive and Antidiabetic Peptides Derived from In Silico Simulated Gastrointestinal Digestion of Quinoa (Chenopodium Quinoa) Globulins and Molecular Docking Study","volume":"47","author":"Chirinosa","year":"2024","journal-title":"Quim. Nova"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"1838","DOI":"10.1007\/s00044-024-03284-2","article-title":"Characterization of Allium Tuberosum Rottl. Peptides with Dual Inhibitory Activities against Angiotensin I Converting Enzyme and Dipeptidyl Peptidase-IV","volume":"33","author":"Nong","year":"2024","journal-title":"Med. Chem. Res."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"142285","DOI":"10.1016\/j.foodchem.2024.142285","article-title":"Chemical Characterization and DPP IV Inhibitory Capacity of Purified Adzuki Bean \u03b2-Vignin Digest in Comparison to Soybean \u03b2-Conglycinin and in Vitro Effect of \u03b2-Vignin on Diabetic-Related Outcomes","volume":"467","author":"Kwan","year":"2025","journal-title":"Food Chem."},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Saetang, J., Haewphet, T., Nilsuwan, K., and Benjakul, S. (2025). ACE- and DPP-IV-Inhibitory Peptides from Bambara Groundnut Hydrolysate: Elucidation Using Computational Tools and Molecular Docking. Biology, 14.","DOI":"10.3390\/biology14050511"},{"key":"ref_140","doi-asserted-by":"crossref","unstructured":"Shan, Q., Jia, Y., Wu, T., Zhang, J., and Shan, L. (2025). Seabuckthorn Seed Meal Protein-Based Inhibitory Peptides Targeting Multiple Hyperglycemic Enzymes: Optimization of Process and Probing of Mechanisms. Foods, 14.","DOI":"10.3390\/foods14111876"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"107416","DOI":"10.1016\/j.fbio.2025.107416","article-title":"Identification, Screening, and Mechanistic Analysis of Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Peptides from Walnut (Juglans regia L.) Protein","volume":"71","author":"Jiang","year":"2025","journal-title":"Food Biosci."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"144530","DOI":"10.1016\/j.foodchem.2025.144530","article-title":"Preparation, Identification, and Molecular Mechanism of Novel DPP-IV Inhibitory Peptides from Pumpkin Seed: In Silico Screening and Experimental Validation","volume":"486","author":"Chen","year":"2025","journal-title":"Food Chem."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Abida, S.H., Sutopo, C.C.Y., Hung, W.-T., Nong, N.T.P., Mahatmanto, T., and Hsu, J.-L. (2025). Stable Non-Competitive DPP-IV Inhibitory Hexapeptide from Parkia timoriana Seeds: A Candidate for Functional Food Development in Type 2 Diabetes. Processes, 13.","DOI":"10.3390\/pr13103079"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"144979","DOI":"10.1016\/j.foodchem.2025.144979","article-title":"DPP-IV Inhibitory Peptides from Highland Barley via Machine Learning and Multi-Scale Validation","volume":"489","author":"Bao","year":"2025","journal-title":"Food Chem."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1002\/jsfa.70156","article-title":"Design and Experimental Verification of Novel Angiotensin-Converting Enzyme and Dipeptidyl Peptidase IV Inhibitory Peptides from Ziziphus jujuba Peptide KALVAP","volume":"106","author":"Wen","year":"2026","journal-title":"J. Sci. Food Agric."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"10221","DOI":"10.1021\/acs.jafc.2c03949","article-title":"Rapid Screening of Novel Dipeptidyl Peptidase-4 Inhibitory Peptides from Pea (Pisum sativum L.) Protein Using Peptidomics and Molecular Docking","volume":"70","author":"Zhang","year":"2022","journal-title":"J. Agric. Food Chem."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"130888","DOI":"10.1016\/j.foodchem.2021.130888","article-title":"Generation, Characterization and Molecular Binding Mechanism of Novel Dipeptidyl Peptidase-4 Inhibitory Peptides from Sorghum bicolor Seed Protein","volume":"369","author":"Majid","year":"2022","journal-title":"Food Chem."}],"container-title":["Pharmaceutics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4923\/18\/6\/741\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T08:41:38Z","timestamp":1781685698000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4923\/18\/6\/741"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,15]]},"references-count":147,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2026,6]]}},"alternative-id":["pharmaceutics18060741"],"URL":"https:\/\/doi.org\/10.3390\/pharmaceutics18060741","relation":{},"ISSN":["1999-4923"],"issn-type":[{"value":"1999-4923","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,15]]}}}