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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.
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:
References
Creative Peptides has accumulated a huge library of peptide knowledge including frontier peptide articles, application of peptides, useful tools, and more!
Muramyl dipeptide (MDP) is the smallest structural unit with immune activity in the skeleton of bacille calmette ...
APETx2, a 42 amino-acid peptide toxin isolated from sea anemone Anthopleura elegantissima, is a kind of acid-s ...
The sodium channel subtypes NaV1.2 and NaV1.6 are the two major forms of excitatory pyramidal neurons in the cer ...
Purotoxin 1, a component from the venom of Geolycosa spiders, exerts selective inhibitory action on P2X3 recep ...
PR 39, a porcine 39-aa peptide antibiotic, was originally isolated from the upper part of the small intestine o ...