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The most reactive base propenal, adenine propenal, is mutagenic in Escherichia coli and reacts with DNA to form covalent adducts; however, the reaction of adenine propenal with protein has not yet been investigated. A survey of the reaction of adenine propenal with amino acids revealed that lysine and cysteine form adducts, whereas histidine and arginine do not. N\u03b5-Oxopropenyllysine, a lysine\u2013lysine cross-link, and S-oxopropenyl cysteine are the major products. Comprehensive profiling of the reaction of adenine propenal with human serum albumin and the DNA repair protein, XPA, revealed that the only stable adduct is N\u03b5-oxopropenyllysine. The most reactive sites for modification in human albumin are K190 and K351. Three sites of modification of XPA are in the DNA-binding domain, and two sites are subject to regulatory acetylation. Modification by adenine propenal dramatically reduces XPA\u2019s ability to bind to a DNA substrate.<\/jats:p>","DOI":"10.1021\/tx500218g","type":"journal-article","created":{"date-parts":[[2014,9,24]],"date-time":"2014-09-24T10:40:59Z","timestamp":1411555259000},"page":"1732-1742","source":"Crossref","is-referenced-by-count":8,"title":["Protein Modification by Adenine\nPropenal"],"prefix":"10.1021","volume":"27","author":[{"given":"Sarah C.","family":"Shuck","sequence":"first","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Orrette R.","family":"Wauchope","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kristie L.","family":"Rose","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philip J.","family":"Kingsley","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carol A.","family":"Rouzer","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven M.","family":"Shell","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]},{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Norie","family":"Sugitani","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]},{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Walter J.","family":"Chazin","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]},{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]},{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irene","family":"Zagol-Ikapitte","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olivier","family":"Boutaud","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John A.","family":"Oates","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]},{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James J.","family":"Galligan","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William N.","family":"Beavers","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lawrence J.","family":"Marnett","sequence":"additional","affiliation":[{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]},{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]},{"name":"Vanderbilt University School of Medicine , , , , , , , ,","place":["Nashville, Tennessee, United States, 37232-0146"]},{"name":"Vanderbilt University 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Clin. Invest."},{"key":"2026092806072658500_cit2","doi-asserted-by":"crossref","first-page":"8652","DOI":"10.1073\/pnas.94.16.8652","article-title":"Mutagenicity in Escherichia coli of the major DNA adduct derived from the endogenous\nmutagen malondialdehyde","volume":"94","author":"Fink","year":"1997","journal-title":"Proc. Natl. Acad. Sci.\nU.S.A."},{"key":"2026092806072658500_cit3","doi-asserted-by":"crossref","first-page":"8415","DOI":"10.1021\/bi1009024","article-title":"In vitro bypass of the major malondialdehyde-\nand base propenal-derived DNA adduct by human Y-family DNA polymerases\nkappa, iota, and Rev1","volume":"49","author":"Maddukuri","year":"2010","journal-title":"Biochemistry"},{"key":"2026092806072658500_cit4","doi-asserted-by":"crossref","first-page":"8766","DOI":"10.1021\/bi401103k","article-title":"Replication, repair, and translesion\npolymerase bypass of N6-oxopropenyl-2\u2032-deoxyadenosine","volume":"52","author":"Maddukuri","year":"2013","journal-title":"Biochemistry"},{"key":"2026092806072658500_cit5","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1006\/taap.1999.8788","article-title":"4-Hydroxynonenal\nand malondialdehyde hepatic protein adducts in rats treated with carbon\ntetrachloride: immunochemical detection and lobular localization","volume":"161","author":"Hartley","year":"1999","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"2026092806072658500_cit6","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1021\/tx960181b","article-title":"Prooxidant-initiated lipid peroxidation\nin isolated rat hepatocytes: detection of 4-hydroxynonenal\u2013\nand malondialdehyde\u2013protein adducts","volume":"10","author":"Hartley","year":"1997","journal-title":"Chem. Res. Toxicol."},{"key":"2026092806072658500_cit7","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.bbrc.2008.03.140","article-title":"Site-specific modification\nof positively-charged surfaces on human serum albumin by malondialdehyde","volume":"371","author":"Ishii","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2026092806072658500_cit8","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1021\/tx050231p","article-title":"Mass spectroscopic\ncharacterization of protein modification by malondialdehyde","volume":"19","author":"Ishii","year":"2006","journal-title":"Chem. Res. Toxicol."},{"key":"2026092806072658500_cit9","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1006\/abbi.1997.0266","article-title":"Protein modification\nby lipid peroxidation products: formation of malondialdehyde-derived N\u03b5-(2-propenol)lysine in proteins","volume":"346","author":"Uchida","year":"1997","journal-title":"Arch. Biochem. Biophys."},{"key":"2026092806072658500_cit10","first-page":"125","article-title":"Malondialdehyde, a major endogenous\nlipid peroxidation product, sensitizes human cells to UV- and BPDE-induced\nkilling and mutagenesis through inhibition of nucleotide excision\nrepair","volume":"601","author":"Feng","year":"2006","journal-title":"Mutat. Res."},{"key":"2026092806072658500_cit11","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1038\/nrc1652","article-title":"Cancer\nin xeroderma pigmentosum and related disorders of DNA repair","volume":"5","author":"Cleaver","year":"2005","journal-title":"Nat. Rev. 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Toxicol."},{"key":"2026092806072658500_cit16","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1038\/nrc1547","article-title":"Bleomycins: towards\nbetter therapeutics","volume":"5","author":"Chen","year":"2005","journal-title":"Nat. Rev. Cancer"},{"key":"2026092806072658500_cit17","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.abb.2003.12.017","article-title":"Reactive\nnitrogen species in the chemical biology of\ninflammation","volume":"423","author":"Dedon","year":"2004","journal-title":"Arch. Biochem. Biophys."},{"key":"2026092806072658500_cit18","doi-asserted-by":"crossref","first-page":"25377","DOI":"10.1074\/jbc.M503079200","article-title":"Chemical and biological evidence\nfor base propenals as the major source of the endogenous M1dG adduct\nin cellular DNA","volume":"280","author":"Zhou","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2026092806072658500_cit19","doi-asserted-by":"crossref","first-page":"1480","DOI":"10.1073\/pnas.91.4.1480","article-title":"Detoxication\nof base propenals and other alpha, beta-unsaturated aldehyde products\nof radical reactions and lipid peroxidation by human glutathione transferases","volume":"91","author":"Berhane","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026092806072658500_cit20","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1002\/mas.20006","article-title":"Proteins as\nbiomarkers of oxidative\/nitrosative stress in diseases: the contribution\nof redox proteomics","volume":"24","author":"Dalle-Donne","year":"2005","journal-title":"Mass Spectrom. Rev."},{"key":"2026092806072658500_cit21","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.mam.2011.12.002","article-title":"Human serum albumin:\nfrom bench to bedside","volume":"33","author":"Fanali","year":"2012","journal-title":"Mol. Aspects Med."},{"key":"2026092806072658500_cit22","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1016\/j.freeradbiomed.2004.09.017","article-title":"Biomarkers of oxidative\nstress study II: are oxidation products of lipids, proteins, and DNA\nmarkers of CCl4 poisoning?","volume":"38","author":"Kadiiska","year":"2005","journal-title":"Free Radical Biol.\nMed."},{"key":"2026092806072658500_cit23","doi-asserted-by":"crossref","first-page":"e85216","DOI":"10.1371\/journal.pone.0085216","article-title":"Cys34-cysteinylated\nhuman serum albumin is a sensitive plasma marker in oxidative stress-related\nchronic diseases","volume":"9","author":"Nagumo","year":"2014","journal-title":"PLoS One"},{"key":"2026092806072658500_cit24","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1021\/tx400384e","article-title":"Mass spectrometric methods for the\nanalysis of nucleoside-protein cross-links: application to oxopropenyl-deoxyadenosine","volume":"27","author":"Shuck","year":"2014","journal-title":"Chem. Res. Toxicol."},{"key":"2026092806072658500_cit25","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.molcel.2010.07.006","article-title":"SIRT1 regulates\nUV-induced DNA repair through deacetylating XPA","volume":"39","author":"Fan","year":"2010","journal-title":"Mol. Cell"},{"key":"2026092806072658500_cit26","doi-asserted-by":"crossref","first-page":"954","DOI":"10.1021\/jm00374a004","article-title":"Synthesis\nand biological activity of a new class of cytotoxic agents: N-(3-oxoprop-1-enyl)-substituted pyrimidines and purines","volume":"27","author":"Johnson","year":"1984","journal-title":"J. Med. Chem."},{"key":"2026092806072658500_cit27","doi-asserted-by":"crossref","first-page":"3030","DOI":"10.1021\/ja00401a020","article-title":"Degenerative chemistry of malondialdehyde.\nStructure, stereochemistry, and kinetics of formation of enaminals\nfrom reaction with amino acids","volume":"103","author":"Nair","year":"1981","journal-title":"J. Am. 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Chem."},{"key":"2026092806072658500_cit48","unstructured":"Galligan, J.\n           Unpublished results."},{"key":"2026092806072658500_cit34","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1093\/protein\/12.6.439","article-title":"Crystal structure\nof human serum albumin at 2.5 \u00c5 resolution","volume":"12","author":"Sugio","year":"1999","journal-title":"Protein Eng."},{"key":"2026092806072658500_cit35","doi-asserted-by":"crossref","first-page":"15988","DOI":"10.1073\/pnas.252550199","article-title":"Identification\nof specific HIV-1 reverse transcriptase contacts to the viral RNA:tRNA\ncomplex by mass spectrometry and a primary amine selective reagent","volume":"99","author":"Kvaratskhelia","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026092806072658500_cit36","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1021\/bi048208a","article-title":"Mass spectrometric\nidentification of lysines involved in the interaction of human replication\nprotein a with single-stranded DNA","volume":"44","author":"Shell","year":"2005","journal-title":"Biochemistry"},{"key":"2026092806072658500_cit37","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/S0009-8981(03)00003-2","article-title":"Protein carbonyl\ngroups as biomarkers of oxidative stress","volume":"329","author":"Dalle-Donne","year":"2003","journal-title":"Clin.\nChim. Acta"},{"key":"2026092806072658500_cit38","doi-asserted-by":"crossref","first-page":"1714","DOI":"10.1021\/tx100186t","article-title":"Protein adducts\nas prospective biomarkers of nevirapine toxicity","volume":"23","author":"Antunes","year":"2010","journal-title":"Chem. Res. Toxicol."},{"key":"2026092806072658500_cit39","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1002\/jmr.734","article-title":"Broadly distributed\nnucleophilic reactivity of proteins coordinated with specific ligand\nbinding activity","volume":"18","author":"Nishiyama","year":"2005","journal-title":"J. Mol. Recognit."},{"key":"2026092806072658500_cit40","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1124\/mol.65.3.655","article-title":"Protein\nadduct-trapping by hydrazinophthalazine drugs: mechanisms of cytoprotection\nagainst acrolein-mediated toxicity","volume":"65","author":"Burcham","year":"2004","journal-title":"Mol. Pharmacol."},{"key":"2026092806072658500_cit41","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1021\/tx950153d","article-title":"Mechanism of acetaminophen-induced\nhepatotoxicity: covalent binding versus oxidative stress","volume":"9","author":"Gibson","year":"1996","journal-title":"Chem. Res. Toxicol."},{"key":"2026092806072658500_cit42","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.jchromb.2012.12.033","article-title":"Identification and quantification of drug-albumin adducts\nin serum samples from a drug exposure study in mice","volume":"917\u2013918","author":"Switzar","year":"2013","journal-title":"J. Chromatogr. B: Anal. Technol. Biomed. Life Sci."},{"key":"2026092806072658500_cit43","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1002\/jms.1067","article-title":"Mass spectrometric characterization\nof covalent modification of human serum albumin by 4-hydroxy-trans-2-nonenal","volume":"41","author":"Aldini","year":"2006","journal-title":"J. Mass Spectrom."},{"key":"2026092806072658500_cit44","doi-asserted-by":"crossref","first-page":"10521","DOI":"10.1021\/bi060535q","article-title":"Covalent adduction\nof human serum albumin by 4-hydroxy-2-nonenal: kinetic analysis of\ncompeting alkylation reactions","volume":"45","author":"Szapacs","year":"2006","journal-title":"Biochemistry"},{"key":"2026092806072658500_cit45","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1021\/tx7001405","article-title":"Identification of\nthe protein targets of the reactive metabolite of teucrin A in vivo\nin the rat","volume":"20","author":"Druckova","year":"2007","journal-title":"Chem. Res. Toxicol."},{"key":"2026092806072658500_cit46","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1007\/978-0-387-09599-8_4","article-title":"XPA gene, its product\nand biological roles","volume":"637","author":"Camenisch","year":"2008","journal-title":"Adv. Exp. Med. Biol."},{"key":"2026092806072658500_cit47","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1007\/978-0-387-09599-8_2","article-title":"Clinical features of\nxeroderma pigmentosum","volume":"637","author":"Hengge","year":"2008","journal-title":"Adv. Exp. Med. 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