Defining the structural characteristics of annexin V binding to a mimetic apoptotic membrane

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dc.contributor.authorLu, JXen_AU
dc.contributor.authorLe Brun, APen_AU
dc.contributor.authorChow, SHen_AU
dc.contributor.authorShiota, Ten_AU
dc.contributor.authorWang, Ben_AU
dc.contributor.authorLin, TWen_AU
dc.contributor.authorLiu, GSen_AU
dc.contributor.authorShen, HHen_AU
dc.date.accessioned2025-06-27T04:17:01Zen_AU
dc.date.available2025-06-27T04:17:01Zen_AU
dc.date.issued2015-08-14en_AU
dc.date.statistics2024-09-03en_AU
dc.description.abstractAnnexin V is of crucial importance for detection of the phosphatidylserine of apoptotic cell membranes. However, the manner in which different amounts of phosphatidylserine at the membrane surface at different stages of apoptosis contribute to binding of annexin V is unclear. We have used a quartz crystal microbalance combined with dissipative monitoring (QCM–D) and neutron reflectivity to characterize binding of human annexin V to supported bilayers of different phospholipid composition. We created model apoptotic bilayers of 1-palmitoyl-2-oleoyl-sn-glycerophosphocholine and 1-palmitoyl-2-oleoyl-sn-glycerophosphoserine (POPS) in the ratios 19:1, 9:1, 6.7:1, 4:1, 3:1, and 2:1 (w/w) in the presence of 2.5 mM CaCl2. QCM–D data revealed that annexin V bound less to supported fluid lipid bilayers with higher POPS content (>25 % POPS). Neutron reflectivity was used to further characterize the detailed composition of lipid bilayers with membrane-bound annexin V. Analysis confirmed less annexin V binding with higher POPS content, that bound annexin V formed a discrete layer above the lipid bilayer with little effect on the overall structure of the membrane, and that the thickness and volume fraction of the annexin V layer varied with POPS content. From these results we show that the POPS content of the outer surface of lipid bilayers affects the structure of membrane-bound annexin V. © 2024 Springer Nature.en_AU
dc.description.sponsorshipWe thank the Australian Nuclear Science and Technology Organisation for allocation of beam time (proposal ID: P882) to this project. We gratefully acknowledge support by the Australian Research Council (ARC) for research funding through the Discovery Early Career Researcher Award grant DE140101788 (to APLB) and NHMRC Program Grant APP1047603 (to HHS). The authors declare no competing financial interest.en_AU
dc.format.mediumPrint-Electronicen_AU
dc.identifier.citationLu, J., Le Brun, A. P., Chow, S. H., Shiota, T., Wang, B., Lin, T.-W., Liu, G.-S., & Shen, H.-H. (2015). Defining the structural characteristics of annexin V binding to a mimetic apoptotic membrane. European Biophysics Journal, 44(8), 697-708. doi:10.1007/s00249-015-1068-zen_AU
dc.identifier.issn0175-7571en_AU
dc.identifier.issn1432-1017en_AU
dc.identifier.issue8en_AU
dc.identifier.journaltitleEuropean Biophysics Journalen_AU
dc.identifier.pagination697-708en_AU
dc.identifier.urihttps://doi.org/10.1007/s00249-015-1068-zen_AU
dc.identifier.urihttps://apo.ansto.gov.au/handle/10238/16208en_AU
dc.identifier.volume44en_AU
dc.languageEnglishen_AU
dc.language.isoenen_AU
dc.publisherSpringer Natureen_AU
dc.subjectMembranesen_AU
dc.subjectVanadiumen_AU
dc.subjectCell membranesen_AU
dc.subjectApoptosisen_AU
dc.subjectQuartzen_AU
dc.subjectNeutron reflectorsen_AU
dc.subjectMicrobalancesen_AU
dc.subjectLipidsen_AU
dc.subjectPhospholipidsen_AU
dc.subjectProteinsen_AU
dc.titleDefining the structural characteristics of annexin V binding to a mimetic apoptotic membraneen_AU
dc.typeJournal Articleen_AU
dcterms.dateAccepted2015-07-29en_AU
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