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Protein immobilization on liposomes and lipid‐coated nanoparticles by protein trans ‐splicing
Author(s) -
Chu Nam Ky,
Olschewski Diana,
Seidel Ralf,
Winklhofer Konstanze F.,
Tatzelt Jörg,
Engelhard Martin,
Becker Christian F. W.
Publication year - 2010
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1227
Subject(s) - intein , chemistry , trans splicing , peptide , liposome , native chemical ligation , vesicle , protein splicing , recombinant dna , biochemistry , target protein , pegylation , combinatorial chemistry , membrane , rna splicing , biophysics , gene , biology , cysteine , enzyme , rna , polyethylene glycol
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. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.