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Synthesis of a GPI anchor module suitable for protein post‐translational modification
Author(s) -
Schumacher Miria C.,
Resenberger Ulrike,
Seidel Ralf P.,
Becker Christian F. W.,
Winklhofer Konstanze F.,
Oesterhelt Dieter,
Tatzelt Jörg,
Engelhard Martin
Publication year - 2010
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21380
Subject(s) - chemistry , posttranslational modification , function (biology) , biochemistry , glycosyl , peptide , microbiology and biotechnology , enzyme , biology
Eukaryotic cell surface proteins are often modified by a glycosylphosphatidylinositol (GPI) anchor. More than 200 of these post‐translationally altered proteins are presently known, a prominent example being the prion protein (PrP). Although the significance of the GPI anchor is well recognized, efforts to study its function are hampered due to its complex chemical nature, which combines hydrophilic glycosyl chains with hydrophobic lipid moieties. Here we describe a general method for the synthesis of a GPI‐anchored peptide containing an N‐terminal Cys. This module can be employed for the production of proteins containing a natural GPI anchor using expressed protein ligation. © 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 94: 457–464, 2010.