Chemical aminoacylation of tRNAs with fluorinated amino acids for in vitro protein mutagenesis

• Shijie Ye,
• Allison Ann Berger,
• Dominique Petzold,
• Oliver Reimann,
• Benjamin Matt and
• Beate Koksch

Beilstein J. Org. Chem. 2010, 6, No. 40, doi:10.3762/bjoc.6.40

• -83855644 10.3762/bjoc.6.40 Abstract This article describes the chemical aminoacylation of the yeast phenylalanine suppressor tRNA with a series of amino acids bearing fluorinated side chains via the hybrid dinucleotide pdCpA and ligation to the corresponding truncated tRNA species. Aminoacyl-tRNAs can be

• protein environment and to enable the design of fluorinated proteins with arbitrary desired properties. Keywords: chemical aminoacylation; DfeGly; fluorinated amino acids; site-specific protein mutagenesis; TfeGly; TfmAla; Introduction Over the past two decades, the interest in engineering proteins

• cyanomethyl ester was achieved in an overall yield of 22%. The syntheses of N-(4-pentenoyl) amino acid cyanomethyl esters are summarized in Table 1. Syntheses of 2′(3′)-O-[N-(4-pentenoyl)aminoacyl]-tRNAs and bis-2′,3′-O-[N-(4-pentenoyl)aminoacyl]-tRNAs Chemical aminoacylation of pdCpA [4] was carried out