Abstract
Abstract Genetic code manipulation enables the ribosomal synthesis of peptide libraries bearing diverse nonproteinogenic amino acids, which can be applied to the discovery of bioactive peptides in combination with screening methodologies, such as mRNA display. Despite a tremendous number of successes in incorporation of l-α-amino acids with non-proteinogenic sidechains and N-methyl-l-α-amino acids into nascent peptide chains, d-, β-, and γ-amino acids have suffered from low translation efficiency. This obstacle has been hindering their integration into such peptide libraries. However, the use of engineered tRNAs, which can effectively recruit EF-Tu or/and EF-P, has recently made possible significant improvement of their incorporation efficiency into nascent peptides. This article comprehensively summarizes advances in such methodology and applications to the discovery of peptide ligands against target proteins of interest.
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