AnaSpec Offers Custom Synthesis of Hydrocarbon-Stapled Peptides
San Jose, CA, June 20, 2008 --(PR.com)-- 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.
Company Info
AnaSpec, Inc. is a leading provider of integrated proteomics solutions to pharmaceutical, biotech, and academic research institutions throughout the world. With a vision for innovation through synergy, AnaSpec focuses on three core technologies: peptides, detection reagents (dyes, assay kits, & antibodies), and combinatorial chemistry.
For more information, visit www.anaspec.com
References:
Walensky, LD. et al. Science 305, 1466 (2004).
Schafmeister, CE. et al. J. Am. Chem. Soc. 122, 5891 (2002).
Qiu, W. et al. Tetrahedron 56, 2577 (2000).
Belokon, Y. N. et al. Tetrahedron: Asymmetry 9, 4249 (1998).
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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.
Company Info
AnaSpec, Inc. is a leading provider of integrated proteomics solutions to pharmaceutical, biotech, and academic research institutions throughout the world. With a vision for innovation through synergy, AnaSpec focuses on three core technologies: peptides, detection reagents (dyes, assay kits, & antibodies), and combinatorial chemistry.
For more information, visit www.anaspec.com
References:
Walensky, LD. et al. Science 305, 1466 (2004).
Schafmeister, CE. et al. J. Am. Chem. Soc. 122, 5891 (2002).
Qiu, W. et al. Tetrahedron 56, 2577 (2000).
Belokon, Y. N. et al. Tetrahedron: Asymmetry 9, 4249 (1998).
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Contact
AnaSpec, Inc.
Ping Yang
408-452-5055
www.anaspec.com
Ping Yang
408-452-5055
www.anaspec.com
Contact
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