Application examples of enzymatic synthesis of polypeptides

Enzymatic synthesis method has long been used not only to synthesize a series of N-protected amino acid hydrazides and other small peptide protective peptide esters, amides and peptides, but also to synthesize some bioactive peptides and semi synthesis of proteins and their analogues.

1. Synthesis of enkephalin and Val angiotensin II

Kurman reasonably used a-chymotrypsin to synthesize Leu enkephalin and Met enkephalin. In these reactions, the solubility of reactants is good, but the solubility of products is poor, which is also conducive to synthetic reactions.

Isova et al. synthesized protected Va1 antihypertensive peptide and antihypertensive peptide with papain, bacterial metalloproteinase and Nagarse.

2. Enzymatic Synthesis and Enzymatic Semisynthesis of Soybean Trypsin Inhibitors and Analogues

Soybean trypsin inhibitor is a protein rich in 181 amino acids and two disulfide bonds. Raskowski experiment learned that; Molecules broken by the cleavage of STI trypsin at Arg Ile can also obtain re synthesized proteins under the catalysis of trypsin.

3. Enzymatic Synthesis and Enzymatic Semisynthesis of Pancreatic Vasopressin Inhibitors and Their Analogues

Jeriog and Tschesche first added NaBH4 to inhibit vasodilator, conditionally restored two disulfide bonds, and then cut and oxidized with trypsin to restore disulfide bonds, and then re synthesized and semi synthesized.

4. Resynthesis and Semi synthesis of Insulin and Its Analogues

Insulin is a protein molecule consisting of a 21 amino acid A chain and a 30 amino acid B chain connected by two disulfide bonds. Its A chain itself has a disulfide bond. (Insulin is the main therapeutic drug for diabetes, and it is also the first artificially synthesized protein. Therefore, many laboratories have conducted extensive research on the relationship between its structure and function by means of chemical total synthesis, semi synthesis and enzymatic semi synthesis.)