6533b86cfe1ef96bd12c8c5f
RESEARCH PRODUCT
Functionalized lipid tubules as tools for helical crystallization of proteins
Philippe RinglerAlain BrissonWolfgang MüllerHelmut Ringsdorfsubject
StreptavidinliposomesSupramolecular chemistryTWO-DIMENSIONAL CRYSTALSMEMBRANESCatalysisACETYLCHOLINE-RECEPTORVESICLESlipidschemistry.chemical_compoundTOXIN B-SUBUNITMolecular recognition2-DIMENSIONAL CRYSTALLIZATIONELECTRON-MICROSCOPYLiposomeChemistryVesicleOrganic Chemistrytechnology industry and agricultureCHOLERA-TOXINGeneral ChemistryCrystallographyMembranehelical structuresRESOLUTIONBiotinylationSelf-assemblyself-assembly tubulesMICROSTRUCTURESdescription
The development of functional supramolecular devices built by self-assembly of elementary molecules and with bioactive properties arouses considerable interest in the field of nanotechnology and new materials. We report here the formation of a new class of lipid tubules exhibiting both properties of molecular recognition and crystal formation for the protein streptavidin. These lipid tubules, made of biotin-containing dioctadecylamine molecules, are straight hollow cylinders with a constant diameter of 27 nm and variable length up to several micrometers. They are unilamellar with an inner diameter of about 16 nm, as shown by cryoelectron microscopy. Streptavidin binds to the biotinylated tubules and assembles spontaneously into ordered helical arrays at the tube surface. These crystals exhibit regular order up to about 1.5 nm resolution, In addition, the helical streptavidin arrays act as functionalized supramolecular devices that bind a wide variety of biotinylated objects, as demonstrated here with proteins and liposomes.
year | journal | country | edition | language |
---|---|---|---|---|
1997-04-01 | Chemistry – A European Journal |