| Home > Publications Database > Protein immobilization on liposomes and lipid-coated nanoparticles by protein trans-splicing. |
| Journal Article | DZNE-2020-02436 |
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2010
Wiley
New York, NY [u.a.]
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Please use a persistent id in citations: doi:10.1002/psc.1227
Abstract: A plethora of methods exist to link proteins to surfaces in order to generate functionalized materials. However, general tools that lead to functional immobilization of recombinantly expressed proteins on membranes such as liposomes or lipid-coated nanoparticles are rare. Here we present an approach that takes advantage of a double-palmitoylated peptide that mediates stable membrane anchoring in combination with protein trans-splicing for efficient immobilization of recombinant proteins fused to split intein segments. Two different DnaE split inteins from Synechocystis and Nostoc punctiforme are tested and compared to immobilization via direct native chemical ligation using a protein thioester. Protein trans-splicing proceeds at low protein concentrations and leads to functionalized vesicles and membrane-coated silica nanoparticles.
Keyword(s): Immobilized Proteins: chemistry (MeSH) ; Immobilized Proteins: metabolism (MeSH) ; Inteins: genetics (MeSH) ; Lipids: chemistry (MeSH) ; Liposomes: metabolism (MeSH) ; Models, Molecular (MeSH) ; Nanoparticles: chemistry (MeSH) ; Nostoc: genetics (MeSH) ; Protein Splicing (MeSH) ; Recombinant Fusion Proteins: chemistry (MeSH) ; Recombinant Fusion Proteins: genetics (MeSH) ; Recombinant Fusion Proteins: metabolism (MeSH) ; Synechocystis: genetics (MeSH) ; Trans-Splicing (MeSH) ; Immobilized Proteins ; Lipids ; Liposomes ; Recombinant Fusion Proteins
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