The innovative technique of hydrocarbon stapling in peptides is introducing valuable new functionality to peptide-related research. AnaSpec is pleased to offer custom synthesis for hydrocarbon-stapled peptides.
Hydrocarbon-stapled peptides are peptides capable of forming stable alpha helical structure as a result of “hydrocarbon stapling.”1,2 Many biological pathways, such as signal transduction, occur because of intracellular protein-protein interactions, which frequently are mediated by the a-helix structures of proteins; however, the use of short protein fragments (peptides) leads to a loss of secondary structure, such as alpha helical structure. Short peptides are easily degraded by proteolysis and have difficulty in intact cells penetration.1 Verdine’s group has shown that these problems could be overcome by a chemical modification of an alpha-helical peptide they termed hydrocarbon-stapled peptide.1,2 The modified hydrocarbon-stapled peptide is helical, relatively protease resistant, cell-permeable and binds with increased binding affinity to its target. Hydrocarbon stapling may provide a useful strategy in researching experimental and therapeutic modulation of protein-protein interactions as well as in in vivo pharmacokinetics studies.
AnaSpec presented a poster on hydrocarbon-stapled peptides last year at the 20th American Peptide Society. Click icon in "Detailed information" to download the PDF
Figure 1. Strategy for hydrocarbon-stapled peptide with enhanced α-helical structure.
1. Walensky, LD. et al. Science305, 1466 (2004). 2. Schafmeister, CE. et al. J. Am. Chem. Soc.122, 5891 (2002). 3.Qiu, W. et al. Tetrahedron56, 2577 (2000). 4. Belokon, Y. N. et al. Tetrahedron: Asymmetry9, 4249 (1998).
Poster
