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SoftMatter
ROYALSOCIETYOFCHEMISTRY
P
P
APER
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OpenAccessArticle.Publishedon09January2025.Downloadedon3/4/20259:15:03PM.Citethis:Soft
OpenAccessArticle.Publishedon09January2025.Downloadedon3/4/20259:15:03PM.
Received29thAugust2024,Accepted7thJanuary2025
DOI:10.1039/d4sm01036arsc.li/soft-matter-journal
a-SynucleininteractionwithPOPC/POPSvesicles?
MarijaDubackic,*aVeronicaLattanzi,abYunLiu,cdMichaelHaertlein,eJulietteM.Devos,eEmmaSparr,aSaraLinsebandUlfOlssona
Wehaveinvestigatedtheadsorptionoftheamyloid-formingproteina-Synuclein(aSyn)ontosmallunilamellarvesiclescomposedofamixtureofzwitterionicPOPCandanionicPOPSlipids.aSynmono-mersadsorbontotheanioniclipidvesicleswheretheyadoptana-helicalsecondarystructure.Thedegreeofadsorptiondependsonthefractionofanioniclipidinthemixedlipidmembrane,butoneneedstoconsidertheelectrostaticshiftoftheserinepKawithincreasingfractionofPOPS.ThevesicleswithadsorbedaSynmonomersarekineticallystable.However,afterfibrilshavebeenformed,heretriggeredbytheadditionofasmallconcentrationofpre-formedfibrils(seeds),weobservedthattheaveragevesiclesizeincreasedbyapproximatelyafactoroftwo.Thisincreaseinthevesiclesizecanbeexplainedbyvesiclefusiontakingplaceduringthefibrilformationprocess.
1Introduction
a-Synuclein(aSyn)isa140aminoacidresidueslong,intrinsi-callydisorderedprotein,abundantlypresentinneurons.Mono-mericaSyninsolutionhasarandomcoilconformation.However,whenassociatedwithlipidmembranes,apartoftheproteinmoleculecanadoptana-helicalstructure1,2and,undercertainconditions,theproteincanself-assembleintoamyloidfibrilsbyarrangingpartofitssequenceintoβ-strands.3
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