Abstract
Chemoenzymatic peptide synthesis is the hydrolase-catalyzed stereoselective formation of peptide bonds. It is a clean and mild procedure, unlike conventional chemical synthesis, which involves complicated and laborious protection-deprotection procedures and harsh reaction conditions. The chemoenzymatic approach has been utilized for several decades because determining the optimal conditions for conventional synthesis is often time-consuming. The synthesis of poly- and oligopeptides comprising various amino acids longer than a dipeptide continues to pose a challenge owing to the lack of knowledge about enzymatic mechanisms and owing to difficulty in optimizing the pH, temperature, and other reaction conditions. These drawbacks limit the applications of the chemoenzymatic approach. Recently, a variety of enzymes and substrates produced using recombinant techniques, substrate mimetics, and optimal reaction conditions (e.g., frozen aqueous media and ionic liquids) have broadened the scope of chemoenzymatic peptide syntheses. In this review, we highlight the recent advances in the chemoenzymatic syntheses of various peptides and their use in developing new materials and biomedical applications.
Highlights
Linear and circular peptides play important roles in biological reactions and are considered important target molecules for pharmaceutical, nutritional, and cosmetic applications [1]
Poly-L-cysteine was synthesized by α-chymotrypsin chemoenzymatically in a frozen aqueous solution serving as a metal chelating agent, which is still being tested for the removal of toxic metals from wastewater and polluted soils [25]
We have showcased the recent advances in chemoenzymatic peptide synthesis and have discussed the corresponding reaction mechanisms, reaction conditions, and versatile applications of the synthesized peptides
Summary
Linear and circular peptides play important roles in biological reactions and are considered important target molecules for pharmaceutical, nutritional, and cosmetic applications [1]. Various methods for synthesizing peptides have been developed These include solid phase peptide synthesis (SPPS) and recombinant bacterial expression systems [2,3]. Proteases can be utilized for hydrolyzing proteins, they function in the reverse direction, thereby facilitating peptide synthesis. This phenomenon has been known since the middle of the 20th century [5,6]. We have described the engineered reaction conditions as well as the properties of peptides for the development of new materials and biomedical applications
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