| 초록 |
It is well known that standard peptides, which comprise proteinogenic amino acids, can act as specific chemicalprobes to target proteins with high affinity. Despite this fact, a number of peptide drug leads have been abandoned because of their poor cell permeability and protease instability. On the other hand, nonstandard peptides isolated as natural productsoften exhibit remarkable pharmaco-behavior and stability in vivo. Although it is likely that numerous nonstandard therapeutic peptides capable of recognizing various targets could have been synthesized, enzymes for nonribosomal peptide syntheses are complex; therefore, it is difficult to engineer such modular enzymes to build nonstandard peptide libraries. HereIintroduce an emerging technology for the synthesis of nonstandard peptides that employs an integrated system of reconstituted cell-free translation and flexizymes. The historical background of this technology will be summarized and tscurrent and future applications to the synthesis of nonstandard peptides and drug discovery will be discussed. |
