1. In vitro genetic code reprogramming and expansion to study protein function and discover macrocyclic peptide ligands
- Author
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Nicolas A Abrigo, Matthew Ct Hartman, Stacie L. Richardson, Emil S. Iqbal, and Kara K. Dods
- Subjects
0301 basic medicine ,Macrocyclic Compounds ,Peptide ,Computational biology ,Ligands ,Protein Engineering ,010402 general chemistry ,Peptides, Cyclic ,01 natural sciences ,Biochemistry ,Article ,Analytical Chemistry ,Sense Codon ,03 medical and health sciences ,Peptide Library ,Drug Discovery ,Animals ,Humans ,Codon degeneracy ,Codon ,Peptide library ,chemistry.chemical_classification ,Chemistry ,Proteins ,Translation (biology) ,Genetic code ,Stop codon ,0104 chemical sciences ,Amino acid ,030104 developmental biology ,Genetic Code ,Protein Biosynthesis ,Peptides - Abstract
The ability to introduce non-canonical amino acids into peptides and proteins is facilitated by working within in vitro translation systems. Non-canonical amino acids can be introduced into these systems using sense codon reprogramming, stop codon suppression, and by breaking codon degeneracy. Here, we review how these techniques have been used to create proteins with novel properties and how they facilitate sophisticated studies of protein function. We also discuss how researchers are using in vitro translation experiments with non-canonical amino acids to explore the tolerance of the translation apparatus to artificial building blocks. Finally, we give several examples of how non-canonical amino acids can be combined with mRNA-displayed peptide libraries for the creation of protease-stable, macrocyclic peptide libraries for ligand discovery.
- Published
- 2018
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