Keywords: Farnesylation, Lipidation, Molecular Sieves, Multi Derivatization, Peptide Thioalkylation, Lipidated Peptide, Peptide Derivative, Ras Protein, Unclassified Drug, Amino Acid Sequence, Analytical Equipment, Article, One Pot Synthesis, Priority Journal, Protein Processing, Protein Synthesis, Protein Thioalkylation
Affiliations: *** IBB - CNR ***
Institute of Biostructures and Bioimaging, National Research Council, 80134 Naples, Italy
Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, United States
References: Not available.
Lipidated Peptides Via Post-Synthetic Thioalkylation Promoted By Molecular Sieves
A thioalkylation procedure, which uses molecular sieves to promote the reaction, was exploited to provide peptides with useful functional groups (lipidic moieties), naturally occurring on proteins as post-translational modifications. The procedure was further implemented to synthesize tailor-made lipidated peptides, interesting tools to investigate biological processes involving their Ras parent proteins. Moreover, the one-pot preparation of multi-alkylated peptides confirms the versatility and flexibility of the employed methodology. 2014 Springer-Verlag
Lipidated Peptides Via Post-Synthetic Thioalkylation Promoted By Molecular Sieves