ORGN 602 |
| Solid phase peptide synthesis (SPPS) is the standard method of peptide synthesis and is necessary when incorporating unnatural amino acids to a peptide sequence. However, SPPS is limited by significant errors and low yield occurring in peptide sequences of more than 20-30 amino acid residues. For this reason we are exploring a ribosome-mediated biosynthetic pathway which will incorporate the synthetic bucky-amino acid (Baa) to a peptide sequence. Initially, the hybrid dinucleotide pdCpA was chemically synthesized and aminoacylated with the synthetic bucky-amino acid. Misacylation is used to ligate pdCpA-Baa to a truncated suppressor tRNACUA(-CA) to make a chemically aminoacylated suppressor tRNA capable of translation. This process attempts to afford site-specific incorporation of a synthetic amino acid to a peptide sequence through ribosome-mediated biosynthesis of a synthetic peptide including bucky-amino acid in the sequence. |
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New Reactions and Methodology, Heterocycles and Aromatics, Bioorganic Chemistry
8:00 PM-10:00 PM, Tuesday, 12 September 2006 Moscone Center -- Hall D, Poster
Sci-Mix
Division of Organic Chemistry |