(1888PressRelease)
September 19, 2009 - Fremont, CA –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.
References:
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).
About AnaSpec
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
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