Abstract
N,S-diprotected l-thiothreonine and l-allo-thiothreonine derivatives were synthesized using a novel chemical strategy, and used for esterification of the dinucleotide pdCpA. The aminoacylated dinucleotides were then employed for the preparation of activated suppressor tRNA CUA transcripts. Thiothreonine and allo-thiothreonine were incorporated into a predetermined position of a catalytically competent dihydrofolate reductase (DHFR) analogue lacking cysteine, and the elaborated proteins were derivatized site-specifically at the thiothreonine residue with a fluorophore.
Original language | English (US) |
---|---|
Pages (from-to) | 2679-2689 |
Number of pages | 11 |
Journal | Bioorganic and Medicinal Chemistry |
Volume | 20 |
Issue number | 8 |
DOIs | |
State | Published - Apr 15 2012 |
Keywords
- Aminoacylation
- Fluorescence labeling
- Protein synthesis
- Sulfur-containing amino acids
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Pharmaceutical Science
- Drug Discovery
- Clinical Biochemistry
- Organic Chemistry