2017
Reversible stacking of lipid nanodiscs for structural studies of clotting factors
Grushin K, White M, Stoilova-McPhie S. Reversible stacking of lipid nanodiscs for structural studies of clotting factors. Nanotechnology Reviews 2017, 6: 139-148. DOI: 10.1515/ntrev-2016-0073.Peer-Reviewed Original ResearchMembrane scaffold proteinND populationMembrane-associated proteinsDifferent membrane scaffold proteinsSize of nanodiscsDiscoidal phospholipid bilayerLipid nanodiscsLipid ratioCryo-EMBiophysical studiesMacromolecular compositionFunctional studiesNanodiscsLipid compositionStructural studiesPhospholipid bilayersProteinMillimolar concentrationsCa2Lipid mixturesMSP1D1ND formMicroscopy studiesElectron microscopy studiesPopulation
2014
Lipid nanotechnologies for structural studies of membrane‐associated proteins
Stoilova‐McPhie S, Grushin K, Dalm D, Miller J. Lipid nanotechnologies for structural studies of membrane‐associated proteins. Proteins Structure Function And Bioinformatics 2014, 82: 2902-2909. PMID: 24957666, PMCID: PMC5292012, DOI: 10.1002/prot.24631.Peer-Reviewed Original ResearchConceptsMembrane-associated proteinsLipid nanotechnologyLipid nanotubesAqueous solutionStructural studiesStructure determinationCryo-EMND technologiesCryo-electron microscopyLipid nanodisksScaffold proteinMembrane curvatureMacromolecular organizationRich membranesLipid bilayersPhysiological environmentProteinNanotechnologyLipid compositionNanotubesPhysiological conditionsAtomic structureFunctional structureProof of principleNanodisksHelical organization of blood coagulation factor VIII on lipid nanotubes.
Miller J, Dalm D, Koyfman A, Grushin K, Stoilova-McPhie S. Helical organization of blood coagulation factor VIII on lipid nanotubes. Journal Of Visualized Experiments 2014 PMID: 24961276, PMCID: PMC4126079, DOI: 10.3791/51254.Peer-Reviewed Original ResearchConceptsCryo-electron microscopyFVIII formsThree-dimensional structure analysisMembrane-bound stateMembrane-bound structuresSerine protease factor IXaBlood coagulation factor VIIIHelical organizationDeficiency of FVIIISequence proteinFunctional complexLipid nanotubesCryo-EMDetailed protocolProteolytic activationLipid nanotechnologyStructure analysisCoagulation factor VIIIFVIII bindsPowerful approachProteinFunctional structureStructural informationPlatelet membranesMembraneLack of recombinant factor VIII B‐domain induces phospholipid vesicle aggregation: implications for the immunogenicity of factor VIII
Grushin K, Miller J, Dalm D, Parker E, Healey J, Lollar P, Stoilova-McPhie S. Lack of recombinant factor VIII B‐domain induces phospholipid vesicle aggregation: implications for the immunogenicity of factor VIII. Haemophilia 2014, 20: 723-731. PMID: 24750465, PMCID: PMC4149818, DOI: 10.1111/hae.12421.Peer-Reviewed Original ResearchConceptsFVIII formsB domainFVIII-BDDPhospholipid vesicle aggregationFactor VIII B domainCryo-electron microscopyMembrane-bound statePhospholipid vesiclesMembrane-bound formSerine protease factor IXaPhysiological conditionsFVIII B domainSecondary structure distributionCryo-EMVesicle aggregationBiophysical propertiesCircular dichroismProtein therapeuticsVesiclesTenase complexPhospholipid membranesPlatelet surfaceHuman factor VIIIFactor IXaHereditary bleeding disorders