Restricting α-synuclein transport into mitochondria by inhibition of α-synuclein–VDAC complexation as a potential therapeutic target for Parkinson’s disease treatment
Rajendran M, Queralt-Martín M, Gurnev P, Rosencrans W, Rovini A, Jacobs D, Abrantes K, Hoogerheide D, Bezrukov S, Rostovtseva T. Restricting α-synuclein transport into mitochondria by inhibition of α-synuclein–VDAC complexation as a potential therapeutic target for Parkinson’s disease treatment. Cellular And Molecular Life Sciences 2022, 79: 368. PMID: 35718804, PMCID: PMC11072225, DOI: 10.1007/s00018-022-04389-w.Peer-Reviewed Original ResearchConceptsVoltage-dependent anion channelVDAC poreProtein-membrane bindingRegulating mitochondrial functionProximity ligation assayInvolvement of alpha-synucleinMembrane bindingMitochondrial respirationMitochondrial functionHeLa cellsLigation assayLipid membranesHexokinase 2MitochondriaTranslocation processComplex inhibitionAnion channelFluorescence correlation spectroscopyAlpha-synucleinMolecular levelMitochondrial toxicityASynTranslocationPeptide therapeuticsTherapeutic targetTuning protein half-life in mouse using sequence-defined biopolymers functionalized with lipids
Vanderschuren K, Arranz-Gibert P, Khang M, Hadar D, Gaudin A, Yang F, Folta-Stogniew E, Saltzman WM, Amiram M, Isaacs FJ. Tuning protein half-life in mouse using sequence-defined biopolymers functionalized with lipids. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2103099119. PMID: 35046019, PMCID: PMC8794819, DOI: 10.1073/pnas.2103099119.Peer-Reviewed Original ResearchConceptsSequence-defined biopolymersProtein-based drugsModel fusion proteinProof of conceptSynthetic biopolymersBroad applicationsMaterials scienceProgrammable approachLow toxicityHigh specificityPeptide therapeuticsBiopolymersLimited side effectsConjugation sitesBlood serumBiotechnologyTechnical foundationFusion proteinMouse serumBiophysical propertiesAzidophenylalanineApplicationsPast decadeTherapeutics
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