title: Lipidated peptides via post-synthetic thioalkylation promoted by molecular sieves.
abstract: 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.
authors.affiliation: Institute of Biostructures and Bioimaging, National Research Council, 80134, Naples, Italy.
authors.forename: Enrica
authors.initials: E
authors.lastname: Calce
authors.forename: Marilisa
authors.initials: M
authors.lastname: Leone
authors.forename: Luca
authors.initials: L
authors.lastname: Monfregola
authors.forename: Stefania
authors.initials: S
authors.lastname: De Luca
mesh_terms: D000478:Alkylation; D000595:Amino Acid Sequence; D008055:Lipids / Q000737:chemistry; D054878:Lipoylation; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000138:chemical synthesis* / Q000378:metabolism*; D017368:Protein Prenylation; D011499:Protein Processing, Post-Translational; D018631:ras Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D008055:Lipids; D010455:Peptides; D018631:ras Proteins