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Cyclic peptide compounds are a class of cyclic compounds with special structure, widely biological activity and unique mechanism of action, which play an important role in natural products. Cyclic peptides are compounds of stable and uniform conformation in peptide molecules, which have high selective affinity for receptors, strong metabolic stability, and high oral availability. As a drug molecule, a cyclic peptide compound has a wide range of biological activities such as anticancer, antiviral, antibacterial, antifungal, and enzyme inhibitors. Therefore, research on cyclic peptide drugs is receiving more and more attention.
Cyclic peptide synthesis has proven to be useful for several applications:
- Structural studies of peptides
- Investigation of peptides and their biological function
- Enzyme function and kinetics
Cyclic peptides can be produced chemically by using solid-phase peptide synthesis, enzymatic chemistry, or expressed in microorganisms using DNA recombinant techniques. The team of the Creative Peptides insist on continuous innovation, using amide bonds, disulfide bonds and multiple oxidation bridges to synthesize various cyclic peptides to meet the different needs of customers.
Creative Peptides provides different methods for the synthesis of cyclic peptides:
Backbone cyclic peptides are easily assembled via the formation of an amide bond between the peptides own N-terminus amine and C-terminus carboxylic acid. Our commonly used methods are chemical synthesis and biosynthesis. Creative Peptides perform the reaction with very high yields, and routinely provide over 98% purified cycled peptides.
Side chain-to-side chain cyclization is frequently employed to stabilize and select specific conformations and to reduce susceptibility toward proteolytic degradation. Creative Peptides have the capable to selectively protect, and then deprotect peptide sidechains to allow for the formation of lactam bridges between Lysine or Diaminopropanoic acid, and Glutamic and Aspartic Acids. Creative Peptides can even perform multiple different sites for bridge formation.
CLIPS technology is based on the chemical linkage of a liner peptide precursor onto a molecular scaffold via nucleophilic attack of thiol groups present on the linear peptide precursor, usually as cysteine residues, to activated bromides present on the molecular scaffold. Creative peptides can apply this technique skillfully not only to fix the conformation of a linear unprotected peptide but also contributes to the preparation of polycyclic peptide structures with applications in peptidomimetics.
Disulfide bonds are widely present in hormones, enzymes, and immunoglobulins, and are thought to play an important role in reconstructing the conformation of biologically active peptides. To further enhance biological activity, people often introduce disulfide bonds to modify bioactive peptides. Creative Peptides usually add two cysteine residues to the peptide sequence, and the dilute solution of the peptide undergoes mild oxidation to form the desired intramolecular disulfide bond between the two cysteine residues. Ugi reaction also can be provided.
 Tang, J., He, Y., Chen, H., Sheng, W., & Wang, H. (2017). Synthesis of bioactive and stabilized cyclic peptides by macrocyclization using C (sp 3)–H activation. Chemical science, 8(6), 4565-4570.