{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T17:15:01Z","timestamp":1788455701596,"version":"build-2803163510"},"reference-count":66,"publisher":"American Chemical Society (ACS)","issue":"34","license":[{"start":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T00:00:00Z","timestamp":1786924800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T00:00:00Z","timestamp":1786924800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T00:00:00Z","timestamp":1786924800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/na","name":"NIH","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/na","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Curcumin, a polyphenolic natural product, binds to A\u03b242, a protein involved in Alzheimer\u2019s Disease, to inhibit self-aggregation in vitro. Molecular understanding of the binding is important in designing new molecules to inhibit A\u03b242 aggregation. We performed OH radical footprinting of A\u03b242 in the presence and absence of curcumin by using fast photochemical oxidation of proteins (FPOP), followed by mass spectral analysis, to monitor changes in A\u03b242 protein dynamics in the presence of curcumin. The results reveal that curcumin binding reduces oxidative footprinting at the N-terminus and middle region, indicating binding at these sites. Kinetic modeling of the percentage modification shows a significant change in the aggregation of A\u03b242 in the presence of curcumin, whereby one aggregate population nearly disappears. The [A\u03b242:curcumin] binding complexes were also explored using density functional theory (DFT), optimizating the starting structures at the B3LYP\/6\u201331G(d) level for both the N-terminal\/middle and C-terminal\/middle regions. The structure of the lowest-energy complex has curcumin binding at the N-terminal plus middle regions, and this was validated by reoptimization using 6\u2013311G(d,p) and applying Grimme\u2019s dispersion function (GD3). This structure was further confirmed by reoptimization in aqueous media using the Conductor-like Polarizable Continuum Model (CPCM). The new structure not only accounts for the observed changes in \u2022OH footprinting of the N-terminal, middle, and C-terminal regions but also forecasts how this approach can provide insight into protein aggregation. A molecular-level understanding of the binding site of curcumin with A\u03b242 should be helpful in the design of new aggregation modulators.<\/jats:p>","DOI":"10.1021\/jacs.5c22337","type":"journal-article","created":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T04:02:00Z","timestamp":1787025720000},"page":"36365-36378","source":"Crossref","is-referenced-by-count":0,"title":["Mass\nSpectrometric Footprinting and DFT Calculations\nExplain the Effect of Curcumin on the Aggregation of Amyloid \u03b2\n42 (A\u03b242)"],"prefix":"10.1021","volume":"148","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-2498-3390","authenticated-orcid":true,"given":"George","family":"Mathai","sequence":"first","affiliation":[{"name":"Washington University in St. Louis , , , ,","place":["St. Louis, Missouri, United States, 63130"]},{"name":"Sacred Heart College , Thevara , ,","place":["Kochi, India, 682013"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saketh","family":"Chemuru","sequence":"additional","affiliation":[{"name":"Washington University in St. Louis , , , ,","place":["St. Louis, Missouri, United States, 63130"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3050-8038","authenticated-orcid":true,"given":"Austin B.","family":"Moyle","sequence":"additional","affiliation":[{"name":"Washington University in St. Louis , , , ,","place":["St. Louis, Missouri, United States, 63130"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jong Hee","family":"Song","sequence":"additional","affiliation":[{"name":"Washington University in St. Louis , , , ,","place":["St. Louis, Missouri, United States, 63130"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9791-0999","authenticated-orcid":true,"given":"Don","family":"Rempel","sequence":"additional","affiliation":[{"name":"Washington University in St. Louis , , , ,","place":["St. Louis, Missouri, United States, 63130"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daryl","family":"Giblin","sequence":"additional","affiliation":[{"name":"Washington University in St. Louis , , , ,","place":["St. Louis, Missouri, United States, 63130"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1159-4636","authenticated-orcid":true,"given":"Michael L.","family":"Gross","sequence":"additional","affiliation":[{"name":"Washington University in St. Louis , , , ,","place":["St. Louis, Missouri, United States, 63130"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,17]]},"reference":[{"issue":"6","key":"2026090312085172800_cit1","doi-asserted-by":"publisher","first-page":"595","DOI":"10.15252\/emmm.201606210","article-title":"The amyloid hypothesis\nof Alzheimer\u2019s disease at 25years","volume":"8","author":"Selkoe","year":"2016","journal-title":"Embo\nMol. 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Biochem."},{"key":"2026090312085172800_cit31","doi-asserted-by":"publisher","DOI":"10.1016\/j.electacta.2025.146160","article-title":"Amyloid\u2013\u00df\npeptides interaction\nwith curcumin: AFM and electrochemical characterisation","volume":"525","author":"Chiorcea-Paquim","year":"2025","journal-title":"Electrochim. Acta"},{"issue":"16","key":"2026090312085172800_cit32","doi-asserted-by":"publisher","first-page":"2288","DOI":"10.1016\/j.jmb.2018.03.015","article-title":"Structural\nEnsemble Modulation upon\nSmall-Molecule Binding to Disordered Proteins","volume":"430","author":"Heller","year":"2018","journal-title":"J. Mol. Biol."},{"issue":"5","key":"2026090312085172800_cit33","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1080\/17460441.2020.1732920","article-title":"Discovery\nof drugs that directly target the intrinsically disordered region\nof the androgen receptor","volume":"15","author":"Sadar","year":"2020","journal-title":"Expert Opin. 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