posted 03-23-2009 05:47 PM            

AnaSpec has announced 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).

Many biological pathways, such as signal transduction, occur because of intracellular protein-protein interactions, which frequently are mediated by the á-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 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 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.

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 combinatorial chemistry.

For more information visit www.anaspec.com

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).

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