{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T20:16:33Z","timestamp":1788466593547,"version":"build-2803163510"},"reference-count":72,"publisher":"American Chemical Society (ACS)","issue":"35","license":[{"start":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T00:00:00Z","timestamp":1787011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T00:00:00Z","timestamp":1787011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T00:00:00Z","timestamp":1787011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100000165","name":"Division of Chemistry","doi-asserted-by":"publisher","award":["CHE-2202281"],"award-info":[{"award-number":["CHE-2202281"]}],"id":[{"id":"10.13039\/100000165","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,3]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Dysregulated calcium homeostasis is a hallmark of neurodegenerative disorders, such as Alzheimer\u2019s, Parkinson\u2019s, and Huntington\u2019s diseases. In Alzheimer\u2019s disease (AD), the aggregation of amyloid beta (A\u03b2) peptides at neuronal membranes is shown to be modulated by the presence of Ca2+ ions, yet the molecular mechanism by which Ca2+ reshapes A\u03b2 aggregation at anionic membrane surfaces remains poorly understood. To address this knowledge gap, we employed coarse-grained molecular dynamics simulations to investigate the aggregation of the model amyloidogenic K16LVFFAE22 fragment of A\u03b2 (A\u03b216\u201322), on a mixed bilayer composed of 30% anionic phosphatidylserine (PS) and 70% zwitterionic phosphatidylcholine (PC) (30% POPS, 70% POPC) in the presence of Ca2+ ions. We find that Ca2+ ions screen the surface charge and reduce hydrophobic packing defects at the membrane surface. Since peptide binding is primarily driven by electrostatic interactions between positively charged residues and anionic lipids, followed by hydrophobic interactions, these Ca2+-induced changes delay peptide adsorption onto the bilayer, promoting the formation of larger aggregates in solution that subsequently adsorb as preformed aggregates. This is in contrast with the no-Ca2+ condition, where peptides bind earlier as small oligomers and aggregate on the bilayer. Following adsorption, PS\u2013Ca2+\u2013PS ionic bridges rapidly condense PS lipids around peptide aggregates and reduce their lateral mobility. This leads to larger, less ordered aggregates with shallower insertion and hydrophobic residues exposed to the solution, a structural feature associated with seeding-active aggregates. These findings align with Western blot analyses showing enhanced A\u03b2 aggregation with Ca2+ ions and provide a molecular basis for the observed aggregation behavior. Together, our results provide mechanistic insight into how calcium alters the membrane-mediated aggregation pathway of amyloidogenic peptides, potentially informing therapeutic strategies against amyloid pathology.<\/jats:p>","DOI":"10.1021\/acs.jpcb.6c02606","type":"journal-article","created":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T19:02:17Z","timestamp":1787079737000},"page":"8770-8781","source":"Crossref","is-referenced-by-count":0,"title":["Calcium Reshapes\nA\u03b2 Aggregation at Anionic Lipid\nMembranes"],"prefix":"10.1021","volume":"130","author":[{"given":"Meenal","family":"Jain","sequence":"first","affiliation":[{"name":"University of Maryland , , , ,","place":["College Park, Maryland, United States, 20742"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3824-9787","authenticated-orcid":true,"given":"Silvina","family":"Matysiak","sequence":"additional","affiliation":[{"name":"University of Maryland , , , ,","place":["College Park, Maryland, United States, 20742"]},{"name":"University of Maryland , , , ,","place":["College Park, Maryland, United States, 20742"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,18]]},"reference":[{"key":"2026090315292025400_cit1","doi-asserted-by":"publisher","first-page":"2253","DOI":"10.1016\/j.ccr.2012.04.004","article-title":"Metal ions as modulators of protein\nconformation and misfolding in neurodegeneration","volume":"256","author":"Leal","year":"2012","journal-title":"Coord. 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