{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,28]],"date-time":"2026-07-28T15:03:09Z","timestamp":1785250989318,"version":"3.55.0"},"reference-count":41,"publisher":"American Chemical Society (ACS)","issue":"29","license":[{"start":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T00:00:00Z","timestamp":1784073600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM125853"],"award-info":[{"award-number":["GM125853"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,7,28]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Formation of the \u03b2-amyloid (A\u03b2) plaques is a pathological hallmark of Alzheimer\u2019s disease (AD) and is believed to be a primary cause of dementia in elderly individuals. In the present work, we performed molecular dynamics (MD) simulations on the conformational evolution of A\u03b242 dimers in solution and in a membrane-like environment to explore the folding of A\u03b242 during fibrillation. Particularly, the MD simulation was steered by experimental internuclear distance restraints obtained using solid-state nuclear magnetic resonance (ssNMR) spectroscopy. Our results revealed that several hydrophobic and polar motifs within the A\u03b242 sequence played key roles in the early-stage nucleation process of fibrillation, and these motifs are also the stabilizing agents in the mature fibrils, as judged by the energy contribution. Our results also indicated that the membrane-binding of small A\u03b2 oligomers could modulate their structural evolution pathways toward fibrillation. These findings contributed to a better understanding of the molecular-level structural polymorphisms inherent to A\u03b242 fibrils. Further, the current work demonstrated that the combination of MD simulations with ssNMR-based experimental restraints provided a reliable method for studying structural changes of A\u03b2.<\/jats:p>","DOI":"10.1021\/acsomega.6c05189","type":"journal-article","created":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T17:09:08Z","timestamp":1784135348000},"page":"44425-44433","source":"Crossref","is-referenced-by-count":0,"title":["Molecular Dynamics Simulations of A\u03b242 Dimers with\nSolid-State NMR Restraints Capture the Key Structural\nMotifs in A\u03b242 Fibrillation Pathways"],"prefix":"10.1021","volume":"11","author":[{"given":"Angelo L.","family":"Chu","sequence":"first","affiliation":[{"name":"Thomas Jefferson High School for Science and Technology , 6560 Braddock Road , , ,","place":["Alexandria, Virginia, United States, 22312"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Betty S. L.","family":"Chu","sequence":"additional","affiliation":[{"name":"Thomas Jefferson High School for Science and Technology , 6560 Braddock Road , , ,","place":["Alexandria, Virginia, United States, 22312"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0044-810X","authenticated-orcid":true,"given":"Wei","family":"Qiang","sequence":"additional","affiliation":[{"name":"Binghamton University, The State University of New York , , , ,","place":["Binghamton, New York, United States, 13902"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,7,15]]},"reference":[{"issue":"6","key":"2026072810105391900_cit1","doi-asserted-by":"publisher","first-page":"60","DOI":"10.1186\/alzrt226","article-title":"Amyloid \u03b2-protein oligomers and Alzheimer\u2019s\ndisease","volume":"5","author":"Hayden","year":"2013","journal-title":"Alzheimer\u2019s Res. 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