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

• 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

• metabolic processes [20][21]. We report here the chemical and enzymatic aminoacylation of the yeast phenylalanine suppressor tRNA with a series of fluoroalkylated amino acids for site-specific protein mutagenesis (Figure 2). (RS)-2-amino-2-methyl-3,3,3-trifluoropropanoic acid (α-(Tfm)Ala) [22], (S

• are suitable for in vitro protein mutagenesis. Conclusion and Outlook The efficient chemical and enzymatic synthesis of three novel fluorinated aminoacyl-pdCpAs and Abu-pdCpA and their corresponding charged tRNAs is reported. These aminoacyl-tRNAs can be used for site-specific protein mutagenesis in a