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Peptide C-Terminal Modification
The development and importance of C-terminal modification of peptides
The posttranslational modification of eukaryotic proteins by the addition of isoprenyl lipids at their C-termimi was first observed in the 1970s and 1980s. Since then, more than a hundred proteins have been shown to be modified by C15 farnesyl or C20 geranylgeranyl groups, including most members of the Ras, Rho, and Rab familied of G proteins. The C-terminal of the peptide is synthesized as an amide to neutralize negative charge created by the C-terminal COOH. This modification is added to prevent enzyme degradation, to mimic native proteins, and in some cases to remove hydrogen bonding at the C-terminal of the peptides which may interfere with the assays.
Available C-Terminal Modification Services
Creative Peptides provides multiple peptides of C-terminal modification to meet your custom peptide need. These peptide modifications can be used to create synthetic peptide with the exact conformation of characteristics needed for specific applications.
Below is a list of our available modification (include but not limited to the following):
Creative Peptides specialized in the custom synthesis of C-terminal modification peptides, providing a confidential and efficient service at competitive prices. Every step of peptide synthesis is subject to Creative Peptides’ stringent quality control. Typical delivery specifications include:
- HPLC chromatogram
- Mass spec analysis
- Synthesis repor
- Certificate of Analyses
 Amaya, M., Baranova, A., & van Hoek, M. L. (2011). Protein prenylation: A new mode of host–pathogen interaction. Biochemical and biophysical research communications, 416(1-2), 1-6.
 Kim, K. H., & Seong, B. L. (2001). Peptide amidation: Production of peptide hormonesin vivo andin vitro. Biotechnology and Bioprocess Engineering, 6(4), 244-251.