Chemical protein synthesis, a versatile approach
SB-PEPTIDE has a deep expertise in long peptide to miniprotein synthesis from 50 to 120 amino acids. By using chemical synthesis against recombinant synthesis, SB-PEPTIDE can incorporate about any kind of modifications. For example: non-natural amino acids, selectively conjugated fonctions…
In chemical synthesis, the general rule is that the longest a sequence is, the more difficult the synthesis will be. Peptides from 50 amino acids are generally difficult to obtain. That’s a general rule to illustrate the difficulty. But depending on the sequence, some peptides of 10 amino acids can be impossible to synthesize. Moreover, some peptides of 70 amino acids can be obtained in a single synthesis.
Chemical ligation of peptides
SB-PEPTIDE is employing most advanced technologies and procedures to synthesize long sequences. The company has up to date successfully synthesized peptides with 120 amino acids. SB-PEPTIDE could do more if required. The company has a deep expertise in Native Chemical Ligation (NCL) which allows to produce long peptides in several fragments. They are then ligated to each other to obtain the complete protein. By using various native (thioester, SEA, hydrazide) or non-native (triazole, oxime, thioether) strategies, SB-PEPTIDE has all ressources to try finding a strategy.
NCL technics can not be used for every sequences. It generally requires the presence of cysteines in the sequences whom allowed the ligation reaction. They have to be at strategic positions. SB-PEPTIDE is able to use other amino acids to perform ligations on about any sequences.
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Dawson, P. E.; Muir, T. W.; Clark-Lewis, I.; Kent, S. B. Science (1994)
BACKGROUND: Chemoselective reaction of two unprotected peptide segments gives an initial thioester-linked species. Spontaneous rearrangement of this transient intermediate yields a full-length product with a native peptide bond at the ligation site.
OBJECTIVE: Method of protein synthesis by native chemical ligation
METHOD/RESULTS: The utility of native chemical ligation was demonstrated by the one-step preparation of a cytokine containing multiple disulfides. The polypeptide ligation product was folded and oxidized to form the native disulfide-containing protein molecule. Native chemical ligation is an important step toward the general application of chemistry to proteins.
CONCLUSION: Thus, a simple technique has been devised that allows the direct synthesis of native backbone proteins of moderate size.