{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T08:20:22Z","timestamp":1793866822038,"version":"4.6.1"},"reference-count":92,"publisher":"American Chemical Society (ACS)","issue":"1","license":[{"start":{"date-parts":[[2018,1,10]],"date-time":"2018-01-10T00:00:00Z","timestamp":1515542400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100000065","name":"U.S. Department of Health and Human Services","doi-asserted-by":"publisher","award":["R15 NS090380"],"award-info":[{"award-number":["R15 NS090380"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/na","name":"Gettysburg College","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/na","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/na","name":"Gettysburg College, Howard Hughes Medical Institute","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":[[2018,1,31]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Huntington disease (HD) is an inherited neurodegenerative disease caused by the expansion beyond a critical threshold of a polyglutamine (polyQ) tract near the N-terminus of the huntingtin (htt) protein. Expanded polyQ promotes the formation of a variety of oligomeric and fibrillar aggregates of htt that accumulate into the hallmark proteinaceous inclusion bodies associated with HD. htt is also highly associated with numerous cellular and subcellular membranes that contain a variety of lipids. As lipid homeostasis and metabolism abnormalities are observed in HD patients, we investigated how varying both the sphingomyelin (SM) and ganglioside (GM1) contents modifies the interactions between htt and lipid membranes. SM composition is altered in HD, and GM1 has been shown to have protective effects in animal models of HD. A combination of Langmuir trough monolayer techniques, vesicle permeability and binding assays, and in situ atomic force microscopy (AFM) were used to directly monitor the interaction of a model, synthetic htt peptide and a full-length htt-exon1 recombinant protein with model membranes comprised of total brain lipid extract (TBLE) and varying amounts of exogenously added SM or GM1. The addition of either SM or GM1 decreased htt insertion into the lipid monolayers. However, TBLE vesicles with an increased SM content were more susceptible to htt-induced permeabilization, whereas GM1 had no effect on permeablization. Pure TBLE bilayers and TBLE bilayers enriched with GM1 developed regions of roughened, granular morphologies upon exposure to htt-exon1, but plateau-like domains with a smoother appearance formed in bilayers enriched with SM. Oligomeric aggregates were observed on all bilayer systems regardless of induced morphology. Collectively, these observations suggest that the lipid composition and its subsequent effects on membrane material properties strongly influence htt binding and aggregation on lipid membranes.<\/jats:p>","DOI":"10.1021\/acsomega.7b01472","type":"journal-article","created":{"date-parts":[[2018,1,10]],"date-time":"2018-01-10T12:35:54Z","timestamp":1515587754000},"page":"273-285","source":"Crossref","is-referenced-by-count":40,"title":["Sphingomyelin and GM1 Influence Huntingtin Binding\nto, Disruption of, and Aggregation on Lipid Membranes"],"prefix":"10.1021","volume":"3","author":[{"given":"Maxmore","family":"Chaibva","sequence":"first","affiliation":[{"name":"West Virginia University , , 217 Clark Hall , P.O. Box 6045, , ,","place":["Morgantown, West Virginia, United States, 26505"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiang","family":"Gao","sequence":"additional","affiliation":[{"name":"West Virginia University , , 217 Clark Hall , P.O. Box 6045, , ,","place":["Morgantown, West Virginia, United States, 26505"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pranav","family":"Jain","sequence":"additional","affiliation":[{"name":"West Virginia University , , 217 Clark Hall , P.O. Box 6045, , ,","place":["Morgantown, West Virginia, United States, 26505"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"IV","given":"Warren A.","family":"Campbell","sequence":"additional","affiliation":[{"name":"Gettysburg College , , 300 N. Washington Avenue , Campus Box 0393, , ,","place":["Gettysburg, Pennsylvania, United States, 17325"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shelli L.","family":"Frey","sequence":"additional","affiliation":[{"name":"Gettysburg College , , 300 N. Washington Avenue , Campus Box 0393, , ,","place":["Gettysburg, Pennsylvania, United States, 17325"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5262-1867","authenticated-orcid":true,"given":"Justin","family":"Legleiter","sequence":"additional","affiliation":[{"name":"West Virginia University , , 217 Clark Hall , P.O. Box 6045, , ,","place":["Morgantown, West Virginia, United States, 26505"]},{"name":"West Virginia University , , 1 Medical Center Dr. , P.O. Box 9303, , ,","place":["Morgantown, West Virginia, United States, 26505"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2018,1,10]]},"reference":[{"key":"2026090206382468300_cit1","doi-asserted-by":"publisher","first-page":"971","DOI":"10.1016\/0092-8674(93)90585-E","article-title":"A Novel Gene Containing a Trinucleotide\nRepeat That Is Expanded and Unstable on Huntington\u2019s Disease\nChromosomes","volume":"72","author":"The Huntington\u2019s Disease Collaborative Research Group","year":"1993","journal-title":"Cell"},{"key":"2026090206382468300_cit2","doi-asserted-by":"publisher","first-page":"1990","DOI":"10.1126\/science.277.5334.1990","article-title":"Aggregation of huntingtin\nin neuronal\nintranuclear inclusions and dystrophic neurites in brain","volume":"277","author":"DiFiglia","year":"1997","journal-title":"Science"},{"key":"2026090206382468300_cit3","doi-asserted-by":"publisher","first-page":"14777","DOI":"10.1074\/jbc.m109.093708","article-title":"Mutant\nHuntingtin Fragments Form Oligomers in a Polyglutamine Length-dependent\nManner in Vitro and in Vivo","volume":"285","author":"Legleiter","year":"2010","journal-title":"J. Biol. Chem."},{"key":"2026090206382468300_cit4","doi-asserted-by":"publisher","first-page":"828","DOI":"10.1016\/j.neuron.2009.11.020","article-title":"Serines 13 and 16 Are Critical Determinants of Full-Length\nHuman Mutant Huntingtin Induced Disease Pathogenesis in HD Mice","volume":"64","author":"Gu","year":"2009","journal-title":"Neuron"},{"key":"2026090206382468300_cit5","doi-asserted-by":"publisher","first-page":"466","DOI":"10.1016\/j.jmb.2012.01.030","article-title":"Physical Chemistry\nof Polyglutamine: Intriguing Tales of a Monotonous Sequence","volume":"421","author":"Wetzel","year":"2012","journal-title":"J. Mol. Biol."},{"key":"2026090206382468300_cit6","doi-asserted-by":"publisher","first-page":"1215","DOI":"10.1038\/nsmb860","article-title":"Hsp70 and\nHsp40 attenuate formation of spherical and annular polyglutamine oligomers\nby partitioning monomer","volume":"11","author":"Wacker","year":"2004","journal-title":"Nat. Struct. Mol. 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