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Synthesis of the N‐Terminal Lipohexapeptide of Human G αO ‐Protein and Fluorescent‐Labeled Analogues for Biological Studies
Author(s) -
Cotté Alain,
Bader Benjamin,
Kuhlmann Jürgen,
Waldmann Herbert
Publication year - 1999
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/(sici)1521-3765(19990301)5:3<922::aid-chem922>3.0.co;2-o
Subject(s) - myristoylation , fluorescence , chemistry , cleavage (geology) , biochemistry , protein subunit , fluorescent protein , enzyme , peptide , combinatorial chemistry , stereochemistry , green fluorescent protein , biology , membrane , physics , quantum mechanics , paleontology , fracture (geology) , gene
Lipidated and myristoylated peptides corresponding to the characteristic N‐terminus of the α‐subunit of human G αo protein ( 1 ) are efficiently synthesized by employing the enzymatic removal of the choline ester and the Pd 0 ‐mediated cleavage of the allyl ester as key steps. Fluorescent‐labeled lipopeptides fulfill the requirements for employment in subsequent biological studies.