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Yes, we can manufacture peptides containing single or multiple disulfide bonds. We utilize either orthogonal protecting group strategies or random oxidation methods to produce peptides containing disulfide bonds.
Disulfide bonds are primarily covalent linkages between the thiol (sulfur) groups of two cysteine side chains and are an important post-translational modification (PTM) that plays a key role in stabilizing peptide and protein structures. A missing disulfide bond can often cause a disruption in functionality. Disulfide bonds can also be intramolecular (within the same peptide or protein) or intermolecular (between two separate peptides or proteins).
To form a disulfide bond, random oxidation or folding can be used when the peptide naturally adopts the preferred structure. Venom and toxin peptides often fold well naturally and a few examples are ShK, charybdotoxin, margatoxin, HsTX1, and mu-conotoxin.
On the other hand, an orthogonal strategy is used to make certain the required disulfide bonds are formed in the appropriate positions. We are also very experienced with other common cyclization motifs such as stapling, click-chemistry triazoles, head-to-tail and cyclic thioethers, and other types of constrained peptides.
Read more about disulfide bond peptides in our other articles found here. We also invite you to watch our video, Disulfide-Rich Peptide Production at AmbioPharm, Inc:
References:
https://www.nature.com/articles/srep38572
https://pmc.ncbi.nlm.nih.gov/articles/PMC5367942
https://pmc.ncbi.nlm.nih.gov/articles/PMC6647852
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