0000000000287644

AUTHOR

Germán Rivas

0000-0003-3450-7478

showing 3 related works from this author

Plasmonic nanosensors reveal a height dependence of MinDE protein oscillations on membrane features

2018

6 p.-4 fig.

02 engineering and technologyEscherichia-coli010402 general chemistryCurvature01 natural sciencesBiochemistryCatalysisQuantitative Biology::Subcellular ProcessesColloid and Surface ChemistryNanosensorSpectroscopyPlasmonPhospholipidsHydrophobic residuesPlasmonic nanoparticlesChemistryScatteringSensorsGeneral ChemistryBinding021001 nanoscience & nanotechnology0104 chemical sciencesMembraneMembrane curvatureChemical physics0210 nano-technology
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Plasmonic Nanosensors for the Determination of Drug Effectiveness on Membrane Receptors.

2016

We demonstrate the potential of the NanoSPR (nanoscale surface plasmon resonance sensors) method as a simple and cheap tool for the quantitative study of membrane protein–protein interactions. We use NanoSPR to determine the effectiveness of two potential drug candidates that inhibit the protein complex formation between FtsA and ZipA at initial stages of bacterial division. As the NanoSPR method relies on individual gold nanorods as sensing elements, there is no need for fluorescent labels or organic cosolvents, and it provides intrinsically high statistics. NanoSPR could become a powerful tool in drug development, drug delivery, and membrane studies.

0301 basic medicineDrugMaterials sciencemedia_common.quotation_subjectNanotechnologyCell Cycle Proteins02 engineering and technology03 medical and health sciencesBacterial ProteinsNanosensorEscherichia coliGeneral Materials ScienceSurface plasmon resonancePlasmonmedia_commonEscherichia coli ProteinsSurface Plasmon Resonance021001 nanoscience & nanotechnologyNanostructuresCytoskeletal Proteins030104 developmental biologyMembraneDrug developmentDrug deliveryFtsA0210 nano-technologyCarrier ProteinsProtein BindingACS applied materialsinterfaces
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Plasmonic Nanosensors for Simultaneous Quantification of Multiple Protein–Protein Binding Affinities

2014

Most of current techniques used for the quantification of protein-protein interactions require the analysis of one pair of binding partners at a time. Herein we present a label-free, simple, fast, and cost-effective route to characterize binding affinities between multiple macromolecular partners simultaneously, using optical dark-field spectroscopy and individual protein-functionalized gold nanorods as sensing elements. Our NanoSPR method could easily become a simple and standard tool in biological, biochemical, and medical laboratories.

Models MolecularNanotubesBacteriaChemistryMechanical EngineeringProtein proteinBioengineeringNanotechnologyGeneral ChemistrySurface Plasmon ResonanceCondensed Matter PhysicsCytoskeletal ProteinsBacterial ProteinsNanosensorProtein Interaction MappingGeneral Materials ScienceNanorodGoldPlasmonProtein BindingBinding affinitiesMacromoleculeNano Letters
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