innovative technique of hydrocarbon stapling in peptides is introducing valuable
new functionality to peptide-related research. AnaSpec is pleased to offer
custom synthesis of hydrocarbon-stapled peptides.
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 α-helix
structures of proteins. However, the use of short protein fragments (peptides)
leads to a loss of secondary structure, which makes them susceptible to proteolysis
and impermeable across cell membrane.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
Figure 1. Strategy for
hydrocarbon-stapled peptide with enhanced α-helical structure.
addition to offering stapled peptides [(i and i+4) and (i
and i+7)] custom synthesis service, AnaSpec is very pleased to offer
Fmoc amino acids for use in synthesizing stapled peptides (Table 1).
view a paper from the Journal of Molecular Biology entitled "A Cell-penetrating
Helical Peptide as a Potential HIV-1 Inhibitor," reported by scientists
from the Lindsley F. Kimball Research Institute of the New York Blood Center,
New York Structural Biology, AnaSpec, Inc. and the National Cancer Institute-Frederick,
please click here.
1. Fmoc amino acids for the synthesis of stapled peptides.
1. Walensky, LD. et al. Science 305, 1466 (2004).
2. Schafmeister, CE. et al. J. Am. Chem. Soc. 122, 5891 (2000).
3. Zhang, HT. et al. J. Mol. Biol. 378(3), 565-580 (2008).