{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,18]],"date-time":"2026-04-18T00:17:41Z","timestamp":1776471461307,"version":"3.51.2"},"reference-count":60,"publisher":"AIP Publishing","issue":"14","funder":[{"DOI":"10.13039\/501100005320","name":"Xidian University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005320","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["pubs.aip.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2017,4,14]]},"abstract":"<jats:p>The formation of senile plaques in central neural system resulting from the aggregation of the amyloid \u03b2 (A\u03b2) of 40 and 42 residues is one of the two hallmarks of Alzheimer\u2019s disease. Numerous experiments and computational studies have shown that the aggregation of A\u03b2 peptides in vitro is very complex and depends on many factors such as pH, agitation, temperature, and peptide concentration. The impact of a static electric field (EF) on amyloid peptide aggregation has been much less studied, although EFs may have some applications to treat Parkinson\u2019s disease symptoms. Here, we study the influence of an EF strength of 20 mV\/nm, present in the human brains, on the conformation of the A\u03b229\u201342 dimer. Our 7 \u03bcs non-equilibrium atomistic simulations in aqueous solution show that this field-strength promotes substantially the formation of \u03b2-hairpins, believed to be a very important intermediate state during aggregation. This work also suggests that structural biology experiments conducted under appropriate EF strengths may help reduce the conformational heterogeneity of A\u03b21\u201340\/A\u03b21\u201342 dimers and provide significant insights into their structures that may be disease-causing.<\/jats:p>","DOI":"10.1063\/1.4979866","type":"journal-article","created":{"date-parts":[[2017,4,13]],"date-time":"2017-04-13T13:30:14Z","timestamp":1492090214000},"update-policy":"https:\/\/doi.org\/10.1063\/aip-crossmark-policy-page","source":"Crossref","is-referenced-by-count":22,"title":["Small static electric field strength promotes aggregation-prone structures in amyloid-<i>\u03b2<\/i>(29-42)"],"prefix":"10.1063","volume":"146","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9086-3576","authenticated-orcid":false,"given":"Yan","family":"Lu","sequence":"first","affiliation":[{"name":"Xidian University 1 School of Physics and Optoelectronic Engineering, , Xi\u2019an 710071, China"},{"name":"Wake Forest University 2 Department of Physics, , Winston-Salem, North Carolina 27106, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiao-Feng","family":"Shi","sequence":"additional","affiliation":[{"name":"Xidian University 1 School of Physics and Optoelectronic Engineering, , Xi\u2019an 710071, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2699-829X","authenticated-orcid":false,"suffix":"Jr.","given":"Freddie R.","family":"Salsbury","sequence":"additional","affiliation":[{"name":"Wake Forest University 2 Department of Physics, , Winston-Salem, North Carolina 27106, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Philippe","family":"Derreumaux","sequence":"additional","affiliation":[{"name":"Universite Paris Diderot, Sorbonne Paris Cite 3 Laboratoire de Biochimie Theorique, Institut de Biologie Physico-Chimique (IBPC), UPR9080 CNRS, , 13 Rue Pierre et Marie Curie, 75005 Paris, France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"317","published-online":{"date-parts":[[2017,4,13]]},"reference":[{"key":"2023062600360562500_c1","doi-asserted-by":"publisher","first-page":"595","DOI":"10.15252\/emmm.201606210","article-title":"The amyloid hypothesis of Alzheimer\u2019s disease at 25 years","volume":"8","year":"2016","journal-title":"EMBO Mol. 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