{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T04:35:13Z","timestamp":1787027713547,"version":"build-2736575974"},"reference-count":83,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2021,10,6]],"date-time":"2021-10-06T00:00:00Z","timestamp":1633478400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R35 GM136431"],"award-info":[{"award-number":["R35 GM136431"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Glycation of \u03b1-synuclein (\u03b1Syn), as occurs with aging, has been linked to the progression of Parkinson\u2019s disease (PD) through the promotion of advanced glycation end-products and the formation of toxic oligomers that cannot be properly cleared from neurons. DJ-1, an antioxidative protein that plays a critical role in PD pathology, has been proposed to repair glycation in proteins, yet a mechanism has not been elucidated. In this study, we integrate solution nuclear magnetic resonance (NMR) spectroscopy and liquid atomic force microscopy (AFM) techniques to characterize glycated N-terminally acetylated-\u03b1Syn (glyc-ac-\u03b1Syn) and its interaction with DJ-1. Glycation of ac-\u03b1Syn by methylglyoxal increases oligomer formation, as visualized by AFM in solution, resulting in decreased dynamics of the monomer amide backbone around the Lys residues, as measured using NMR. Upon addition of DJ-1, this NMR signature of glyc-ac-\u03b1Syn monomers reverts to a native ac-\u03b1Syn-like character. This phenomenon is reversible upon removal of DJ-1 from the solution. Using relaxation-based NMR, we have identified the binding site on DJ-1 for glycated and native ac-\u03b1Syn as the catalytic pocket and established that the oxidation state of the catalytic cysteine is imperative for binding. Based on our results, we propose a novel mechanism by which DJ-1 scavenges glyc-ac-\u03b1Syn oligomers without chemical deglycation, suppresses glyc-ac-\u03b1Syn monomer\u2013oligomer interactions, and releases free glyc-ac-\u03b1Syn monomers in solution. The interference of DJ-1 with ac-\u03b1Syn oligomers may promote free ac-\u03b1Syn monomer in solution and suppress the propagation of toxic oligomer and fibril species. These results expand the understanding of the role of DJ-1 in PD pathology by acting as a scavenger for aggregated \u03b1Syn.<\/jats:p>","DOI":"10.3390\/biom11101466","type":"journal-article","created":{"date-parts":[[2021,10,6]],"date-time":"2021-10-06T10:36:57Z","timestamp":1633516617000},"page":"1466","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["DJ-1 Acts as a Scavenger of \u03b1-Synuclein Oligomers and Restores Monomeric Glycated \u03b1-Synuclein"],"prefix":"10.3390","volume":"11","author":[{"given":"Tamr B.","family":"Atieh","sequence":"first","affiliation":[{"name":"Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonathan","family":"Roth","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xue","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4441-8321","authenticated-orcid":false,"given":"Cody L.","family":"Hoop","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean","family":"Baum","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,10,6]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"194","DOI":"10.3390\/biom5010194","article-title":"Advanced Glycation End Products and Oxidative Stress in Type 2 Diabetes Mellitus","volume":"5","author":"Nowotny","year":"2015","journal-title":"Biomolecules"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1111\/j.1749-6632.1992.tb38649.x","article-title":"Role of Glycation in Aging","volume":"663","author":"Lee","year":"1992","journal-title":"Ann. 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