## Abstract Split inteins link their fused peptide or protein sequences with a peptide bond in an autocatalytic reaction called protein __trans__‐splicing. This reaction is becoming increasingly important for a variety of applications in protein semisynthesis, polypeptide circularisation, construct
Protein immobilization on liposomes and lipid-coated nanoparticles by protein trans-splicing
✍ Scribed by Nam Ky Chu; Diana Olschewski; Ralf Seidel; Konstanze F. Winklhofer; Jörg Tatzelt; Martin Engelhard; Christian F. W. Becker
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 284 KB
- Volume
- 16
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.1227
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✦ Synopsis
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. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.
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