Linked Life Data

20862726

Source:http://linkedlifedata.com/resource/pubmed/id/20862726

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2010-9-23
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1099-1387
pubmed:author
pubmed:copyrightInfo
© 2010 European Peptide Society and John Wiley & Sons, Ltd.
pubmed:issnType
Electronic
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
582-8
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Protein immobilization on liposomes and lipid-coated nanoparticles by protein trans-splicing.
pubmed:affiliation
Center for Integrated Protein Science Munich and Technische Universität München, Fakultät Chemie, Garching, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't