Synthesis of the palmitoylated and prenylated C-terminal lipopeptides of the human R- and N-Ras proteins.
For the study of biological phenomena influenced by the R- and N-Ras proteins, characteristic peptides which embody the correct lipid modifications of their parent proteins (palmitoyl thioesters, geranylgeranyl thioethers, and farnesyl thioethers), as well as analogues thereof, may serve as efficient tools. For the construction of such acid- and base labile peptide conjugates the allyl ester was developed as C-terminal protecting group. Allyl esters are cleaved selectively and in high yields from lipidated peptides by Pd(0)-mediated allyl transfer to accepting N- or C-nucleophiles like morpholine and N,N'-dimethylbarbituric acid. This protecting group technique formed the key step in the synthesis of the characteristic S-palmitoylated and S-isoprenylated C-terminus of human R-Ras and human N-Ras proteins, as well as several analogues thereof. Deprotections are so mild that no undesired side reactions of the lipid conjugates are observed.[1]References
- Synthesis of the palmitoylated and prenylated C-terminal lipopeptides of the human R- and N-Ras proteins. Schmittberger, T., Waldmann, H. Bioorg. Med. Chem. (1999) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg