Expanded Set of Amino Acid Analogs for Ribosomal Translation of Unnatural Peptides
Author Information
Author(s): Hartman Matthew C. T., Josephson Kristopher, Lin Chi-Wang, Szostak Jack W.
Primary Institution: Howard Hughes Medical Institute, Department of Molecular Biology, Center for Computational and Integrative Biology, Simches Research Center, Massachusetts General Hospital, Boston, Massachusetts, United States of America
Hypothesis
Can a diverse array of unnatural amino acids be incorporated into peptides by ribosomal translation?
Conclusion
The study demonstrates that over 50 unnatural amino acids can be incorporated into peptides, providing new opportunities for drug-like peptide development.
Supporting Evidence
- Over 90 unnatural amino acids can be enzymatically loaded onto tRNA.
- More than 50 unnatural amino acids were shown to be incorporated into peptides by ribosomal translation.
- The translation apparatus tolerates most side chain derivatives but excludes certain types of amino acids.
Takeaway
Scientists found ways to add special building blocks to proteins, which could help create new medicines.
Methodology
The study used competition assays and peptide translation assays to measure the efficiency of unnatural amino acid incorporation into peptides.
Limitations
The translation apparatus does not tolerate certain amino acid analogs, and some analogs were poorly translated or resulted in heterogeneous mixtures.
Digital Object Identifier (DOI)
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