Fremont, CA, September 20, 2009 --(PR.com
)-- The innovative technique of hydrocarbon stapling in peptides is introducing valuable new functionality to peptide-related research. AnaSpec now offers custom synthesis of 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, 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 studies.
In addition to offering stapled peptides [(i and i+4) and (i and i+7)] custom synthesis service, AnaSpec offers Fmoc amino acids for use in synthesizing stapled peptides; as well as three GO™ (catalog) stapled 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 (2008).
AnaSpec is a leading provider of integrated proteomics solutions to the world’s largest biotech, pharmaceutical, and academic research institutions. With a vision for innovation through synergy, AnaSpec focuses on three core technologies: peptides, detection reagents, and antibodies.
For more information visit www.anaspec.com