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Stapled Peptide Synthesis
What is stabled peptide
Stapled peptide is a full-carbon scaffold with an α-helical structure. The all-carbon scaffold stabilizes the α-helical structure, enhances the interaction between the peptide molecule and the protein, and the peptide can pass through the cell membrane and is not easily hydrolyzed. Stapled peptides have higher physiological activity than previous small molecule drugs and protein analogs.
Advantages of Custom Stapled Peptides
• Better target affinity
• Increased proteolytic resistance and serum half- life
• Increased cell permeability
• Targeting of either extracellular or intracellular proteins
• Viable pharmacokinetics and in vivo stability
The synthesis of stapled peptides is different from that of a common peptide. By use of solid phase methods, the peptide chain is introduced two unnatural amino acids containing an α-methyl group and an α-alkenyl group, and then an olefin metathesis reaction occurs between two unnatural amino acids to constitutes a stable α-helical conformation.
Available Stapled Peptide Synthesis Services
One-component stapling techniques
Using non-native amino acids bearing complimentary side-chain functional groups that can be directly coupled together.
Two-component stapling techniques
Involving a bifunctional linker compound which forms a staple by reacting with two complementary non-native amino acids in the peptide of interest.
Creative Peptides provides efficient and high quality peptide synthesis services while offering different modification services. Every step of peptide synthesis is subject to Creative Peptides’ stringent quality control. Typical delivery specifications include:
• HPLC chromatogram
• Mass spec analysis
• Synthesis report
• Certificate of Analyses
1. Lau, Y. H., De Andrade, P., Wu, Y., & Spring, D. R. (2015). Peptide stapling techniques based on different macrocyclisation chemistries. Chemical Society Reviews, 44(1), 91-102.