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) generally leads to the
loss of secondary structure, such as alpha helical structure. Short peptides
also are easily degraded by proteolysis and have difficulty in intact cells
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 was helical and relatively protease
resistant. The modification resulted in cell-permeable peptides that bind with
increased binding affinity for its target, and may provide a useful strategy
for experimental and therapeutic modulation of protein-protein interactions
in many signaling pathways related to apoptosis in cancer cells as well as in
vivo pharmacokinetics and efficacy in disease models.
AnaSpec is pleased to announce the availability of stapled
helical peptides custom synthesis service. Unnatural amino acid (S5
and R8) substitutions flank three (substitution positions i
and i + 4 using S5 and S5, e.g. XXXXX-S5-XXX-S5-XXXXX)
or six standard amino acids (i and i + 7 using R8 and
S5, e.g. XXXXXX-R8-XXXXXX-S5-XXXXX).
Click here for a quotation
Figure 1. Strategy for hydrocarbon-stapled peptide with
enhanced α-helical structure with S5 and S5.
view a list of Hydrocarbon Stapled Peptides, please click here.
To view a
poster presented at the 20th American Peptide Society, please click
Products and Services:
synthesis of unusual peptides – glycopeptides, dye labeled peptides, FRET
peptides, peptide libraries, peptides with multiple disulfide bonds and heavy-isotope
peptides – one of the world’s largest providers of on-demand catalog peptides.
1. Walensky, LD. et al. Science
305, 1466 (2004).
2. Schafmeister, CE. et al. J.
Am. Chem. Soc. 122, 5891 (2002).
3. Zhang, HT. et al. J. Mol. Biol. 378(3), 565-580