Diverse eukaryotic proteins require the post-translational addition of S-acyl chains to cysteine residues for proper function, a process known as S-palmitoylation, or S-acylation. To study the effects of this lipid moiety, various complex methods have been developed for the preparation of synthetic lipopeptides. In order to facilitate this task, a novel technique employing readily-prepared long-chain acyl thioesters has been devised. Using S-phenylmercapto-palmitoyl thioester as well as other acyl thioesters, the fluorescent-labeled peptide, myristoyl-GCG-caBim, was S-acylated to high stoichiometry at halftimes as short as 20 min. (initial rate of S-acylation of 179.8 +/- 24.7%/hr) in homogeneous solution, without the presence of micelles or vesicles. The chemical reaction occurred regioselectively on cysteine side-chains without modification of serine or lysine derivatives of the peptide. This method was also utilized to selectively S-acylate the fully deprotected Po peptide, IRYCWLRR-NH2. Such an innovative technique should provide a useful scheme for the general synthesis of S-acylated peptides.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.82275 |
| Date | January 2004 |
| Creators | Leung Wai Sang, Stephane, 1980- |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Department of Biochemistry.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 002198774, proquestno: AAIMR12486, Theses scanned by UMI/ProQuest. |
Page generated in 0.0267 seconds