{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,10]],"date-time":"2026-07-10T14:18:07Z","timestamp":1783693087437,"version":"3.55.0"},"reference-count":41,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2020,7,6]],"date-time":"2020-07-06T00:00:00Z","timestamp":1593993600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["2015R1A6A1A03031413"],"award-info":[{"award-number":["2015R1A6A1A03031413"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["2018R1A2B6001753"],"award-info":[{"award-number":["2018R1A2B6001753"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Xanthine oxidase is a frontier enzyme to produce oxidants, which leads to inflammation in the blood. Prenylated isoflavones from Flemingia philippinensis were found to display potent inhibition against xanthine oxidase (XO). All isolates (1\u20139) inhibited XO enzyme with IC50 ranging 7.8~36.4 \u03bcM. The most active isoflavones (2\u20135, IC50 = 7.8~14.8 \u03bcM) have the structural feature of a catechol motif in B-ring. Inhibitory behaviors were disclosed as a mixed type I mode of inhibition with KI &lt; KIS. Binding affinities to XO enzyme were evaluated. Fluorescence quenching effects agreed with inhibitory potencies (IC50s). The compounds (2\u20135) also showed potent anti-LDL oxidation effects in the thiobarbituric acid-reactive substances (TBARS) assay, the lag time of conjugated diene formation, relative electrophoretic mobility (REM), and fragmentation of apoB-100 on copper-mediated LDL oxidation. The compound 4 protected LDL oxidation with 0.7 \u03bcM in TBARS assay, which was 40-fold more active than genistein (IC50 = 30.4 \u03bcM).<\/jats:p>","DOI":"10.3390\/molecules25133074","type":"journal-article","created":{"date-parts":[[2020,7,6]],"date-time":"2020-07-06T11:07:42Z","timestamp":1594033662000},"page":"3074","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Xanthine Oxidase Inhibition and Anti-LDL Oxidation by Prenylated Isoflavones from Flemingia philippinensis Root"],"prefix":"10.3390","volume":"25","author":[{"given":"Jeong Yoon","family":"Kim","sequence":"first","affiliation":[{"name":"Division of Applied Life Science (BK21 Plus), IALS, Gyeongsang National University, Jinju 52828, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2817-1648","authenticated-orcid":false,"given":"Yan","family":"Wang","sequence":"additional","affiliation":[{"name":"College of Food and Biological Engineering, Qiqihar University, Qiqihar 161006, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zuo Peng","family":"Li","sequence":"additional","affiliation":[{"name":"Division of Applied Life Science (BK21 Plus), IALS, Gyeongsang National University, Jinju 52828, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1549-8978","authenticated-orcid":false,"given":"Aizhamal","family":"Baiseitova","sequence":"additional","affiliation":[{"name":"Division of Applied Life Science (BK21 Plus), IALS, Gyeongsang National University, Jinju 52828, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yeong Jun","family":"Ban","sequence":"additional","affiliation":[{"name":"Division of Applied Life Science (BK21 Plus), IALS, Gyeongsang National University, Jinju 52828, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ki Hun","family":"Park","sequence":"additional","affiliation":[{"name":"Division of Applied Life Science (BK21 Plus), IALS, Gyeongsang National University, Jinju 52828, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,7,6]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1456","DOI":"10.1016\/S0891-5849(00)00252-5","article-title":"Reactive oxygen species, cell signaling, and cell injury","volume":"28","author":"Hensley","year":"2000","journal-title":"Free Radic. Biol. Med."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.1089\/ars.2012.5149","article-title":"Reactive oxygen species in inflammation and tissue injury","volume":"20","author":"Mittal","year":"2014","journal-title":"Antioxid. Redox Signal."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1016\/j.atherosclerosis.2014.10.006","article-title":"Xanthine oxidoreductase in atherosclerosis pathogenesis: Not only oxidative stress","volume":"237","author":"Battelli","year":"2014","journal-title":"Atherosclerosis"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1007\/s11906-010-0103-9","article-title":"Oxidative stress and vascular function: Implications for pharmacologic treatments","volume":"12","author":"Weseler","year":"2010","journal-title":"Curr. Hypertens. Rep."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"2557","DOI":"10.1016\/j.bbadis.2018.05.003","article-title":"The role of xanthine oxidoreductase and uric acid in metabolic syndrome","volume":"1864","author":"Battelli","year":"2018","journal-title":"Biochim. Biophys. Acta-Mol. Basis Dis."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.ejim.2015.11.026","article-title":"Uric acid in metabolic syndrome: From an innocent bystander to a central player","volume":"29","author":"Kanbay","year":"2016","journal-title":"Eur. J. Intern. Med."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.niox.2013.02.081","article-title":"Xanthine oxidoreductase-catalyzed reduction of nitrite to nitric oxide: Insights regarding where, when anqd how","volume":"34","author":"Kelley","year":"2013","journal-title":"Nitric Oxide-Biol. Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/j.freeradbiomed.2009.11.012","article-title":"Hydrogen peroxide is the major oxidant product of xanthine oxidase","volume":"48","author":"Kelley","year":"2010","journal-title":"Free Radic. Biol. Med."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1161\/01.RES.87.10.840","article-title":"Endothelial dysfunction in cardiovascular diseases: The role of oxidant stress","volume":"87","author":"Cai","year":"2000","journal-title":"Circ. Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1002\/cmdc.201900034","article-title":"Inhibitors of Xanthine Oxidase: Scaffold Diversity and Structure-Based Drug Design","volume":"14","author":"Luna","year":"2019","journal-title":"ChemMedChem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S0891-5849(03)00239-9","article-title":"Beyond LDL oxidation: ROS in vascular signal transduction","volume":"35","author":"Chen","year":"2003","journal-title":"Free Radic. Biol. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1093\/cvr\/cvx226","article-title":"Endothelial permeability, LDL deposition, and cardiovascular risk factors\u2014A review","volume":"114","author":"Mundi","year":"2018","journal-title":"Cardiovasc. Res."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"152786","DOI":"10.1155\/2013\/152786","article-title":"LOX-1, OxLDL, and atherosclerosis","volume":"2013","author":"Pirillo","year":"2013","journal-title":"Mediat. Inflamm."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.1172\/JCI117776","article-title":"Modified Low Density Lipoprotein and Its Constituents Augment Cytokine-activated Vascular Cell Adhesion Molecule-1 Gene Expression in Human Vascular Endothelial Cells","volume":"95","author":"Khan","year":"1995","journal-title":"J. Clin. Investig."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"158518","DOI":"10.1016\/j.bbalip.2019.158518","article-title":"Low profile high value target: The role of OxLDL in cancer","volume":"1864","author":"Bitorina","year":"2019","journal-title":"Biochim. Biophys. Acta-Mol. Cell Biol. Lipids"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"304","DOI":"10.5551\/jat.E621","article-title":"A uniqe antilipidemic drug\u2014Probucol","volume":"15","author":"Yamamoto","year":"2008","journal-title":"J. Atheroscler. Thromb."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"8563845","DOI":"10.1155\/2019\/8563845","article-title":"Targeting early atherosclerosis: A focus on oxidative stress and inflammation","volume":"2019","author":"Marchio","year":"2019","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"5790291","DOI":"10.1155\/2019\/5790291","article-title":"Flemingia philippinensis Flavonoids Relieve Bone Erosion and Inflammatory Mediators in CIA Mice by Downregulating NF- \u03ba B and MAPK Pathways","volume":"2019","author":"Sun","year":"2019","journal-title":"Mediat. Inflamm."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.1002\/mrc.2336","article-title":"Prenylated isoflavones from Flemingia philippinensis","volume":"46","author":"Li","year":"2008","journal-title":"Magn. Reson. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"6398","DOI":"10.1016\/j.bmc.2013.08.049","article-title":"Bacterial neuraminidase inhibitory effects of prenylated isoflavones from roots of Flemingia philippinensis","volume":"21","author":"Wang","year":"2013","journal-title":"Bioorganic Med. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"7637","DOI":"10.3390\/molecules17077637","article-title":"A New benzofuran derivative from flemingia philippinensis Merr. et Rolfe","volume":"17","author":"Li","year":"2012","journal-title":"Molecules"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/j.bmc.2013.12.047","article-title":"Inhibition of tyrosinase activity by polyphenol compounds from Flemingia philippinensis roots","volume":"22","author":"Wang","year":"2014","journal-title":"Bioorganic Med. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.ijbiomac.2019.01.105","article-title":"Highly potent bacterial neuraminidase inhibitors, chromenone derivatives from Flemingia philippinensis","volume":"128","author":"Wang","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"e1600193","DOI":"10.1002\/cbdv.201600193","article-title":"Chemical Composition of Roots Flemingia philippinensis and Their Inhibitory Kinetics on Aromatase","volume":"14","author":"Sun","year":"2017","journal-title":"Chem. Biodivers."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/j.fitote.2011.01.019","article-title":"A new coumestan with immunosuppressive activities from Flemingia philippinensis","volume":"82","author":"Li","year":"2011","journal-title":"Fitoterapia"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/j.bmcl.2015.12.021","article-title":"Novel chromenedione derivatives displaying inhibition of protein tyrosine phosphatase 1B (PTP1B) from Flemingia philippinensis","volume":"26","author":"Wang","year":"2016","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/j.bioorg.2018.03.024","article-title":"Competitive neutrophil elastase inhibitory isoflavones from the roots of Flemingia philippinensis","volume":"78","author":"Kim","year":"2018","journal-title":"Bioorganic Chem."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Kim, J.Y., Wang, Y., Song, Y.H., Uddin, Z., Li, Z.P., Ban, Y.J., and Park, K.H. (2018). Antioxidant activities of phenolic metabolites from flemingia philippinensis Merr. et rolfe and their application to DNA damage protection. Molecules, 23.","DOI":"10.3390\/molecules23040816"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1016\/j.fct.2018.09.025","article-title":"Effects of auriculasin on vascular endothelial growth factor (VEGF)-induced angiogenesis via regulation of VEGF receptor 2 signaling pathways in vitro and in vivo","volume":"121","author":"Cho","year":"2018","journal-title":"Food Chem. Toxicol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1016\/j.fct.2017.12.007","article-title":"Auriculasin-induced ROS causes prostate cancer cell death via induction of apoptosis","volume":"111","author":"Cho","year":"2018","journal-title":"Food Chem. Toxicol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1111\/j.1432-1033.1969.tb00708.x","article-title":"Substrate Activation with a Xanthine Oxidase Reaction: An Alternative to Dismutation as an Explanation in the Chicken Liver System","volume":"10","author":"Priest","year":"1969","journal-title":"Eur. J. Biochem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/j.jphotobiol.2015.10.022","article-title":"Deciphering the inhibitory mechanism of genistein on xanthine oxidase in vitro","volume":"153","author":"Lin","year":"2015","journal-title":"J. Photochem. Photobiol. B Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"3766","DOI":"10.1016\/j.foodchem.2013.06.092","article-title":"Effect of luteolin on xanthine oxidase: Inhibition kinetics and interaction mechanism merging with docking simulation","volume":"141","author":"Yan","year":"2013","journal-title":"Food Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"102981","DOI":"10.1016\/j.bioorg.2019.102981","article-title":"Investigation of the interaction between salvianolic acid C and xanthine oxidase: Insights from experimental studies merging with molecular docking methods","volume":"88","author":"Tang","year":"2019","journal-title":"Bioorganic Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.jff.2019.05.045","article-title":"Inhibitory effects of compounds isolated from roots of Cynanchum wilfordii on oxidation and glycation of human low-density lipoprotein (LDL)","volume":"59","author":"Kim","year":"2019","journal-title":"J. Funct. Foods"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"2057","DOI":"10.1021\/jf052431c","article-title":"LDL-antioxidant pterocarpans from roots of Glycine max (L) Merr","volume":"54","author":"Jin","year":"2006","journal-title":"J. Agric. Food Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/j.foodchem.2013.09.018","article-title":"Koelreuteria formosana extract impedes in vitro human LDL and prevents oxidised LDL-induced apoptosis in human umbilical vein endothelial cells","volume":"146","author":"Lin","year":"2014","journal-title":"Food Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"950","DOI":"10.1016\/j.foodres.2017.01.023","article-title":"Malaysian brown seaweeds Sargassum siliquosum and Sargassum polycystum: Low density lipoprotein (LDL) oxidation, angiotensin converting enzyme (ACE), \u03b1-amylase, and \u03b1-glucosidase inhibition activities","volume":"99","author":"Nagappan","year":"2017","journal-title":"Food Res. Int."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2343","DOI":"10.1002\/rcm.6361","article-title":"Simultaneous characterization of prenylated flavonoids and isoflavonoids in Psoralea corylifolia L. by liquid chromatography with diode-array detection and quadrupole time-of-flight mass spectrometry","volume":"26","author":"Xu","year":"2012","journal-title":"Rapid Commun. Mass Spectrom."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.foodchem.2013.12.026","article-title":"Quantitative analysis of phenolic metabolites from different parts of Angelica keiskei by HPLC-ESI MS\/MS and their xanthine oxidase inhibition","volume":"153","author":"Kim","year":"2014","journal-title":"Food Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"3435","DOI":"10.1021\/ja01164a032","article-title":"The Quenching of Fluorescence. Deviations from the Stern-Volmer Law","volume":"72","author":"Boaz","year":"1950","journal-title":"J. Am. Chem. Soc."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/25\/13\/3074\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T09:48:11Z","timestamp":1760176091000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/25\/13\/3074"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,7,6]]},"references-count":41,"journal-issue":{"issue":"13","published-online":{"date-parts":[[2020,7]]}},"alternative-id":["molecules25133074"],"URL":"https:\/\/doi.org\/10.3390\/molecules25133074","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,7,6]]}}}