2022
Functionalized DNA-Origami-Protein Nanopores Generate Large Transmembrane Channels with Programmable Size-Selectivity
Shen Q, Xiong Q, Zhou K, Feng Q, Liu L, Tian T, Wu C, Xiong Y, Melia T, Lusk C, Lin C. Functionalized DNA-Origami-Protein Nanopores Generate Large Transmembrane Channels with Programmable Size-Selectivity. Journal Of The American Chemical Society 2022, 145: 1292-1300. PMID: 36577119, PMCID: PMC9852090, DOI: 10.1021/jacs.2c11226.Peer-Reviewed Original ResearchConceptsExchange of macromoleculesCholesterol-rich membranesHybrid nanoporesSynthetic biologyBiophysical toolsSynthetic cellsTransmembrane channelsTransmembrane nanoporesDNA ringsProtein nanoporeCell membraneBacterial toxinsDNA origami techniqueLipid membranesAnalytical chemistryMacromolecule sizeDNA origamiMembraneProgrammable sizeNanoporesSized poresNucleoporinsAverage inner diameterCellsPneumolysinActuating tension-loaded DNA clamps drives membrane tubulation
Liu L, Xiong Q, Xie C, Pincet F, Lin C. Actuating tension-loaded DNA clamps drives membrane tubulation. Science Advances 2022, 8: eadd1830. PMID: 36223466, PMCID: PMC9555772, DOI: 10.1126/sciadv.add1830.Peer-Reviewed Original ResearchConceptsDNA clampMembrane tubulationMembrane dynamicsMembrane-remodeling eventsVesicle tubulationConformational changesSpatiotemporal controlDNA signalsCell membraneDNA nanostructuresTubulationMembrane deformationClosed stateOpen stateSelf-assembled DNA nanostructuresOrganismsProteinMembrane tubeArtificial systemsTube widthMembraneDynamicsFrame-Guided Assembly of Amphiphiles
Dong Y, Yang Y, Lin C, Liu D. Frame-Guided Assembly of Amphiphiles. Accounts Of Chemical Research 2022, 55: 1938-1948. PMID: 35786832, DOI: 10.1021/acs.accounts.2c00234.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsFrame-guided assemblyMolecular structureAssembly of amphiphilesArrangement of moleculesTraditional chemical industryMembrane protein incorporationProtein-lipid bilayerAmphiphilic assembliesAssembly morphologyAmphiphile assembliesFunctional nanomaterialsVersatile strategyAqueous environmentHydrophobic groupsHydrophobic moleculesFull surface areaHydrophobic interactionsAmphiphilesDrug deliveryMembrane proteinsFunctional complexAmphiphile concentrationAssembly strategyEPR effectNanomaterialsOmicron-specific mRNA vaccination alone and as a heterologous booster against SARS-CoV-2
Fang Z, Peng L, Filler R, Suzuki K, McNamara A, Lin Q, Renauer PA, Yang L, Menasche B, Sanchez A, Ren P, Xiong Q, Strine M, Clark P, Lin C, Ko AI, Grubaugh ND, Wilen CB, Chen S. Omicron-specific mRNA vaccination alone and as a heterologous booster against SARS-CoV-2. Nature Communications 2022, 13: 3250. PMID: 35668119, PMCID: PMC9169595, DOI: 10.1038/s41467-022-30878-4.Peer-Reviewed Original ResearchConceptsHeterologous boosterSARS-CoV-2Antibody responseMRNA vaccinesMRNA vaccinationDelta variantOmicron variantType of vaccinationStrong antibody responseMRNA vaccine candidatesVaccine candidatesNeutralization potencyImmune evasionSARS-CoV.Two weeksComparable titersVaccinationVaccineTiters 10MiceOmicronWeeksWA-1LNP-mRNABoosterVariant-specific vaccination induces systems immune responses and potent in vivo protection against SARS-CoV-2
Peng L, Renauer PA, Ökten A, Fang Z, Park JJ, Zhou X, Lin Q, Dong MB, Filler R, Xiong Q, Clark P, Lin C, Wilen CB, Chen S. Variant-specific vaccination induces systems immune responses and potent in vivo protection against SARS-CoV-2. Cell Reports Medicine 2022, 3: 100634. PMID: 35561673, PMCID: PMC9040489, DOI: 10.1016/j.xcrm.2022.100634.Peer-Reviewed Original ResearchConceptsImmune responseImmune cell populationsSARS-CoV-2 spikeAssessment of efficacySARS-CoV-2LNP-mRNABreakthrough infectionsCD8 TImmune profilingMRNA vaccinesPotent protectionT lymphocytesNeutralization activityDelta variantAnimal modelsPotent antibodiesRepertoire diversityCell responsesAuthentic virusSystemic increaseVariant lineagesClonal expansionCell populationsCOVID-19Vaccination
2021
Sorting sub-150-nm liposomes of distinct sizes by DNA-brick-assisted centrifugation
Yang Y, Wu Z, Wang L, Zhou K, Xia K, Xiong Q, Liu L, Zhang Z, Chapman ER, Xiong Y, Melia TJ, Karatekin E, Gu H, Lin C. Sorting sub-150-nm liposomes of distinct sizes by DNA-brick-assisted centrifugation. Nature Chemistry 2021, 13: 335-342. PMID: 33785892, PMCID: PMC8049973, DOI: 10.1038/s41557-021-00667-5.Peer-Reviewed Original ResearchMeSH KeywordsAutophagy-Related Protein 7CentrifugationCholesterolDNALiposomesParticle SizeSNARE Proteins
2019
A programmable DNA-origami platform for studying lipid transfer between bilayers
Bian X, Zhang Z, Xiong Q, De Camilli P, Lin C. A programmable DNA-origami platform for studying lipid transfer between bilayers. Nature Chemical Biology 2019, 15: 830-837. PMID: 31320758, PMCID: PMC6650167, DOI: 10.1038/s41589-019-0325-3.Peer-Reviewed Original ResearchConceptsLipid transferNon-vesicular lipid transportSynaptotagmin-like mitochondrial lipid-binding protein (SMP) domainLipid transportMembrane contact sitesLipid transport proteinsSMP domainImportant physiological roleDNA origami platformProtein domainsUnstructured linkerContact sitesSynaptotagmin-1Förster resonance energy transferPhysiological roleResonance energy transferMechanistic insightsDNA origami nanostructuresAcceptor liposomesStiffness and Membrane Anchor Density Modulate DNA-Nanospring-Induced Vesicle Tubulation
Grome MW, Zhang Z, Lin C. Stiffness and Membrane Anchor Density Modulate DNA-Nanospring-Induced Vesicle Tubulation. ACS Applied Materials & Interfaces 2019, 11: 22987-22992. PMID: 31252462, PMCID: PMC6613048, DOI: 10.1021/acsami.9b05401.Peer-Reviewed Original ResearchConceptsVesicle tubulationMembrane-deforming proteinsDNA-based constructsMembrane anchorArtificial assemblageMembrane bindingSubcellular membranesDNA nanostructuresMembrane affinityTubulationLipid tubulesMembraneDNA nanotechnologyTunable architecturesPeptide densitySurface of liposomesProteinNanostructuresAssemblagesBindingAffinity
2017
Placing and shaping liposomes with reconfigurable DNA nanocages
Zhang Z, Yang Y, Pincet F, Llaguno M, Lin C. Placing and shaping liposomes with reconfigurable DNA nanocages. Nature Chemistry 2017, 9: 653-659. PMID: 28644472, PMCID: PMC5542812, DOI: 10.1038/nchem.2802.Peer-Reviewed Original ResearchConceptsMembrane-bound vesiclesDNA cagesRegulated deformationsDNA nanocagesMembrane curvatureMembrane fusionConformational changesBiological membranesCell membraneLipid bilayer membranesMembrane mechanicsVesiclesDiverse structuresMembraneCellsBilayer membranesVersatile toolDelivery vesiclesToroid shapeLiposome shape
2016
A Programmable DNA Origami Platform to Organize SNAREs for Membrane Fusion
Xu W, Nathwani B, Lin C, Wang J, Karatekin E, Pincet F, Shih W, Rothman JE. A Programmable DNA Origami Platform to Organize SNAREs for Membrane Fusion. Journal Of The American Chemical Society 2016, 138: 4439-4447. PMID: 26938705, PMCID: PMC4950518, DOI: 10.1021/jacs.5b13107.Peer-Reviewed Original ResearchConceptsMembrane fusionSoluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexCore molecular machineryMembrane fusion eventsProtein receptor complexMembrane fusion processMolecular machineryDNA origami platformTarget membraneAuxiliary proteinsIntracellular communicationDocking stepSingle-event levelReceptor complexLipid mixingSmall unilamellar vesiclesLipid bilayersSnareFundamental processesVesiclesUnilamellar vesiclesTraffickingMachineryProteinFusion