{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T06:29:27Z","timestamp":1786343367499,"version":"build-2736575974"},"reference-count":78,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2026,8,9]],"date-time":"2026-08-09T00:00:00Z","timestamp":1786233600000},"content-version":"vor","delay-in-days":8,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["J of Cellular Biochemistry"],"published-print":{"date-parts":[[2026,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Non\u2010enzymatic glycosylation of proteins leads to the formation of advanced glycation end products (AGEs), implicated in oxidative stress and the progression of several chronic diseases. Among the reactive carbonyl compounds, methylglyoxal (MGO) is highly potent in inducing glycoxidative damage by modifying proteins. Herein, we investigated the protective effect of plumbagin, a naphthoquinone derived from\n                    <jats:italic>Plumbago zeylanica<\/jats:italic>\n                    , to counteract MGO\u2010induced glycation of catalase, employing integrated biophysical and computational approaches. AGE\u2010specific fluorescence at 335 and 370\u2009nm, ThT dye fluorescence, and microscopic visualizations confirmed that plumbagin markedly reduces AGEs formation and aggregation. Fluorescence quenching experiments revealed a stable catalase\u2010plumbagin complex formation having binding affinity (\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>a<\/jats:sub>\n                    ): 0.205 \u00d7 10\n                    <jats:sup>6\u2009<\/jats:sup>\n                    M\n                    <jats:sup>\u22121<\/jats:sup>\n                    and a stoichiometry of one binding site (\n                    <jats:italic>n<\/jats:italic>\n                    \u2009\u2248\u20091.1), suggesting a single, specific binding pocket. Isothermal titration calorimetry (ITC) confirmed an exothermic, enthalpy\u2010driven interaction. Molecular dynamics simulations (MDS) analysis displayed a more compact and ordered conformation of complex, as evidenced by reduced Rg, SASA, and RMSF values. H\u2010bonds stabilized the complex without altering the catalytic residues (His74, Asn147, Tyr357). PCA and FEL showed complex remained confined to a single deep energy minimum, indicating enhanced thermodynamic stability. These findings highlight plumbagin as a potent multifunctional compound capable of mitigating MGO\u2010induced glycation.\n                  <\/jats:p>","DOI":"10.1002\/jcb.70117","type":"journal-article","created":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T05:57:52Z","timestamp":1786341472000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Elucidating the Antiglycation Potential of Plumbagin Against Methylglyoxal\u2010Induced Glycation of Bovine Liver Catalase"],"prefix":"10.1002","volume":"127","author":[{"given":"Faiza","family":"Iram","sequence":"first","affiliation":[{"name":"Centre for Interdisciplinary Research in Basic Sciences Jamia Millia Islamia Jamia Nagar New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9257-484X","authenticated-orcid":false,"given":"Ayesha","family":"Aiman","sequence":"additional","affiliation":[{"name":"Centre for Interdisciplinary Research in Basic Sciences Jamia Millia Islamia Jamia Nagar New Delhi India"},{"name":"Department of Biosciences Jamia Millia Islamia Jamia Nagar New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0008-2873-0781","authenticated-orcid":false,"given":"Deepanshi","family":"Vijh","sequence":"additional","affiliation":[{"name":"Agriculture Plant Biotechnology Laboratory University School of Biotechnology, Guru Gobind Singh Indraprastha University Dwarka Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gourav","family":"Choudhir","sequence":"additional","affiliation":[{"name":"Centre for Interdisciplinary Research in Basic Sciences Jamia Millia Islamia Jamia Nagar New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3663-4940","authenticated-orcid":false,"given":"Md. Imtaiyaz","family":"Hassan","sequence":"additional","affiliation":[{"name":"Centre for Interdisciplinary Research in Basic Sciences Jamia Millia Islamia Jamia Nagar New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9060-7970","authenticated-orcid":false,"given":"Asimul","family":"Islam","sequence":"additional","affiliation":[{"name":"Centre for Interdisciplinary Research in Basic Sciences Jamia Millia Islamia Jamia Nagar New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,8,9]]},"reference":[{"issue":"2","key":"e_1_2_13_2_1","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1007\/s12551-024-01188-4","article-title":"An Overview on Glycation: Molecular Mechanisms, Impact on Proteins, Pathogenesis, and Inhibition","volume":"16","author":"Uceda A. B.","year":"2024","journal-title":"Biophysical Reviews"},{"issue":"15","key":"e_1_2_13_3_1","doi-asserted-by":"crossref","first-page":"1653","DOI":"10.2174\/092986707780830989","article-title":"The Road to Advanced Glycation End Products: A Mechanistic Perspective","volume":"14","author":"Cho S.\u2010J.","year":"2007","journal-title":"Current Medicinal Chemistry"},{"issue":"1","key":"e_1_2_13_4_1","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1007\/s11033-025-10632-x","article-title":"Mechanism and Implications of Advanced Glycation End Products (AGE) and Its Receptor RAGE Axis as Crucial Mediators Linking Inflammation and Obesity","volume":"52","author":"Kavitha S. A.","year":"2025","journal-title":"Molecular Biology Reports"},{"issue":"1","key":"e_1_2_13_5_1","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1038\/s41392-022-01251-0","article-title":"Aging and Aging\u2010Related Diseases: From Molecular Mechanisms to Interventions and Treatments","volume":"7","author":"Guo J.","year":"2022","journal-title":"Signal Transduction and Targeted Therapy"},{"key":"e_1_2_13_6_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2024.132859","article-title":"Proteomics\u2010Based Identification of Biomarkers Reflecting Endogenous and Exogenous Exposure to the Advanced Glycation End Product Precursor Methylglyoxal in SH\u2010SY5Y Human Neuroblastoma Cells","volume":"272","author":"Zheng L.","year":"2024","journal-title":"International Journal of Biological Macromolecules"},{"key":"e_1_2_13_7_1","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.cofs.2021.03.011","article-title":"Recent Developments in In\u2010Vitro Assessment of Advanced Glycation End Products","volume":"40","author":"Serin Y.","year":"2021","journal-title":"Current Opinion in Food Science"},{"issue":"5","key":"e_1_2_13_8_1","doi-asserted-by":"crossref","first-page":"E685","DOI":"10.1152\/ajpendo.2001.280.5.E685","article-title":"Activation of NADPH Oxidase by AGE Links Oxidant Stress to Altered Gene Expression via RAGE","volume":"280","author":"Wautier M.\u2010P.","year":"2001","journal-title":"American Journal of Physiology\u2010Endocrinology and Metabolism"},{"issue":"1","key":"e_1_2_13_9_1","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.diabres.2004.09.004","article-title":"Advanced Glycation Endproducts\u2014Role in Pathology of Diabetic Complications","volume":"67","author":"Ahmed N.","year":"2005","journal-title":"Diabetes Research and Clinical Practice"},{"issue":"22","key":"e_1_2_13_10_1","doi-asserted-by":"crossref","first-page":"12090","DOI":"10.1080\/07391102.2023.2267699","article-title":"Antiglycation and Antioxidant Potential of Coumaric Acid Isomers: A Comparative In\u2010Vitro Study","volume":"42","author":"Khan R.","year":"2024","journal-title":"Journal of Biomolecular Structure and Dynamics"},{"issue":"3","key":"e_1_2_13_11_1","doi-asserted-by":"crossref","first-page":"87","DOI":"10.3390\/medsci13030087","article-title":"Pathophysiological Mechanisms of Diabetes\u2010Induced Macrovascular and Microvascular Complications: The Role of Oxidative Stress","volume":"13","author":"Roy B.","year":"2025","journal-title":"Medical Sciences"},{"key":"e_1_2_13_12_1","doi-asserted-by":"crossref","DOI":"10.3389\/fendo.2022.891442","article-title":"Advanced Glycation End\u2010Products Are Associated With Diabetic Neuropathy in Young Adults With Type 1 Diabetes","volume":"13","author":"Al\u2010Saoudi E.","year":"2022","journal-title":"Frontiers in Endocrinology"},{"key":"e_1_2_13_13_1","doi-asserted-by":"crossref","DOI":"10.3389\/fcvm.2023.1094188","article-title":"Glycation of LDL: AGEs, Impact on Lipoprotein Function, and Involvement in Atherosclerosis","volume":"10","author":"Poznyak A. V.","year":"2023","journal-title":"Frontiers in Cardiovascular Medicine"},{"issue":"2","key":"e_1_2_13_14_1","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1042\/BST20140017","article-title":"Prevention of Dicarbonyl\u2010Mediated Advanced Glycation by Glyoxalases: Implication in Skin Aging","volume":"42","author":"Radjei S.","year":"2014","journal-title":"Biochemical Society Transactions"},{"issue":"8","key":"e_1_2_13_15_1","doi-asserted-by":"crossref","first-page":"1312","DOI":"10.3390\/cells11081312","article-title":"Advanced Glycation End\u2010Products (AGEs): Formation, Chemistry, Classification, Receptors, and Diseases Related to AGEs","volume":"11","author":"Twarda\u2010Clapa A.","year":"2022","journal-title":"Cells"},{"issue":"6","key":"e_1_2_13_16_1","doi-asserted-by":"crossref","DOI":"10.1038\/cddis.2013.180","article-title":"Glycation Exacerbates the Neuronal Toxicity of \u03b2\u2010Amyloid","volume":"4","author":"Li X. 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