Unusual and Non-natural Amino Acids Modification

* Please kindly note that our products and services can only be used to support research purposes (Not for clinical use).

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Chemical modifications of peptides introduced strategically at potential enzymatic cleavage sites may dramatically increase the in vivo stability of peptide drug candidates. One simple approach to stabilizing a peptide is to modify the side-chains of some of the amino acids involved in the protease recognition site. The residues of interest are replaced by natural or non-natural amino acids with chemically similar side-chains. The introduction of non-natural amino acids generates modifications in the secondary and tertiary structures of a peptide, and is used to further enhance the stability and activity of peptide sequences.

Functions of unusual & non-natural amino acids modification

• Enhance selectivity
• Improve receptor binding
• Modify bioactivity to target (agonists and antagonists)
• Increase in vivo half-life
• Enhance transportion through cell membranes

Below is a list of our available unusual & non-natural amino acids modification

• D-amino acids
• Homo-amino acids
• Beta-homo-amino acids
• N-methyl amino acids
• Alpha-methyl amino acids
• Unusual amino acids

More than 700 amino acids that are the so-called unusual, unnatural, or nonproteinous amino acids have been found in nature in the free zwitterionic form or as constituents of peptides. These amino acids have attracted much attention from scientists due to their important biological activities as antibiotics, metal chelators, neurotoxins, enzyme inhibitors, etc.

Creative Peptides specialized in the custom synthesis of unusual and non-natural amino acids modification, 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 report
• Certificate of Analyses

References

1. Kiick, K. L., & Tirrell, D. A. (2000). Protein engineering by in vivo incorporation of non-natural amino acids: Control of incorporation of methionine analogues by methionyl-tRNA synthetase.Tetrahedron, 56(48), 9487-9493.
2. Dougherty, D. A. (2000). Unnatural amino acids as probes of protein structure and function.Current opinion in chemical biology, 4(6), 645-652.