2024
DNA-Based Molecular Clamp for Probing Protein Interactions and Structure under Force.
Chung M, Zhou K, Powell JT, Lin C, Schwartz MA. DNA-Based Molecular Clamp for Probing Protein Interactions and Structure under Force. ACS Nano 2024, 18: 27590-27596. PMID: 39344156, DOI: 10.1021/acsnano.4c08663.Peer-Reviewed Original Research In PressDNA-Based Molecular Clamp for Probing Protein Interactions and Structure under Force
Chung M, Zhou K, Powell J, Lin C, Schwartz M. DNA-Based Molecular Clamp for Probing Protein Interactions and Structure under Force. ACS Nano 2024, 18: 27590-27596. PMID: 39344156, DOI: 10.1021/acsnano.4c08663.Peer-Reviewed Original ResearchConceptsTalin rod domainNegative-stain electron microscopyDouble-stranded DNADNA clampProtein functionRod domainCryptic sitesProtein interactionsMolecular clampCellular mechanotransductionStudy proteinsBiochemical studiesCell biologyAdult physiologyProtein conformationTalinProteinBiochemical scaleMultiple diseasesDNAARPC5LVinculinStructural analysisEmbryogenesisDNA-based devices
2023
Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels
Shen Q, Feng Q, Wu C, Xiong Q, Tian T, Yuan S, Shi J, Bedwell G, Yang R, Aiken C, Engelman A, Lusk C, Lin C, Xiong Y. Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels. Nature Structural & Molecular Biology 2023, 30: 425-435. PMID: 36807645, PMCID: PMC10121901, DOI: 10.1038/s41594-023-00925-9.Peer-Reviewed Original ResearchConceptsNuclear pore complexHIV-1 nuclear entryNuclear entryNuclear importNPC central channelPore complexHost nucleusCapsid dockingVirus genomeAffinity gradientNup153Central channelMechanistic insightsMolecular interactionsCapsidNucleoporinsNup358Nup62GenomeNucleusVirusDockingVirus-1 infectionImportComplexes
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 widthMembraneDynamics
2021
DNA-Origami NanoTrap for Studying the Selective Barriers Formed by Phenylalanine-Glycine-Rich Nucleoporins
Shen Q, Tian T, Xiong Q, Fisher P, Xiong Y, Melia TJ, Lusk CP, Lin C. DNA-Origami NanoTrap for Studying the Selective Barriers Formed by Phenylalanine-Glycine-Rich Nucleoporins. Journal Of The American Chemical Society 2021, 143: 12294-12303. PMID: 34324340, PMCID: PMC8363578, DOI: 10.1021/jacs.1c05550.Peer-Reviewed Original ResearchConceptsNuclear pore complexFundamental biological activitiesRich nucleoporinsNuclear transport receptorsSelective barrierPhenylalanine-GlycineStructure-function relationshipsPore complexNuclear transportTransport receptorsProtein assembliesFG-NupsMolecular trafficFG interactionsFG networkBiomolecular machinesNucleoporinsCritical determinantDNA nanotechnologyBiomimetic constructsBiological activityDiffusion barrierModel cargoNanotrapsSpatial arrangementSorting 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 Research
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 liposomes
2018
Vesicle Tubulation with Self‐Assembling DNA Nanosprings
Grome MW, Zhang Z, Pincet F, Lin C. Vesicle Tubulation with Self‐Assembling DNA Nanosprings. Angewandte Chemie International Edition 2018, 57: 5330-5334. PMID: 29575478, PMCID: PMC5924453, DOI: 10.1002/anie.201800141.Peer-Reviewed Original ResearchConceptsMembrane-deforming proteinsDNA origami designMembrane tubulationMembrane tubulesMembrane curvatureMembrane surface coverageVesicle tubulationDNA structureLipid bilayersTubulationNanospringsTube morphologyIntricate interplayArtificial nanomachinesVesicle deformationSpherical vesiclesNanotechnologyMajor goalProteinDNAVesiclesNanomachinesBioengineeringDetergentsMorphologyA Programmable DNA Origami Platform for Organizing Intrinsically Disordered Nucleoporins within Nanopore Confinement
Fisher PDE, Shen Q, Akpinar B, Davis LK, Chung KKH, Baddeley D, Šarić A, Melia TJ, Hoogenboom BW, Lin C, Lusk CP. A Programmable DNA Origami Platform for Organizing Intrinsically Disordered Nucleoporins within Nanopore Confinement. ACS Nano 2018, 12: 1508-1518. PMID: 29350911, PMCID: PMC5834394, DOI: 10.1021/acsnano.7b08044.Peer-Reviewed Original ResearchConceptsTransport channelsAtomic force microscopyMolecular dynamics simulationsHigh-speed atomic force microscopyDNA origami platformFG domainsNuclear pore complexes (NPCs) formChannel mimicsCentral transport channelNuclear pore proteinsForce microscopyDNA origamiNuclear transport receptorsDynamics simulationsSelective transportNanopore confinementMolecular exchangePermeability propertiesDNA cylindersChemical compositionFG networkPore proteinsPolymer modelTransport receptorsCollective properties
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
Self-assembly of size-controlled liposomes on DNA nanotemplates
Yang Y, Wang J, Shigematsu H, Xu W, Shih WM, Rothman JE, Lin C. Self-assembly of size-controlled liposomes on DNA nanotemplates. Nature Chemistry 2016, 8: 476-483. PMID: 27102682, PMCID: PMC5021307, DOI: 10.1038/nchem.2472.Peer-Reviewed Original ResearchConceptsDNA nanotemplatesArtificial lipid bilayer membranesLipid bilayer formationLipid bilayer membranesSelf-AssemblyTemplating methodKey intermediateBilayer formationDrug deliveryArtificial vesiclesLipid compositionNanoscale precisionNanotemplatesHomogeneous liposomesUnilamellar vesiclesLiposome formationVesicular transportProtein structureMembrane structureVesicle sizeLiposomesIntermediatesFormationVesiclesStructure