160711-84-2Relevant academic research and scientific papers
Towards a general method for the stepwise solid-phase synthesis of peptide-oligonucleotide conjugates
Antopolsky, Maxim,Azhayeva, Elena,Tengvall, Unni,Azhayev, Alex
, p. 527 - 530 (2002)
Three peptide-oligonucleotide phosphorothioate hybrids were synthesized using a new approach for stepwise solid-phase synthesis of conjugates. This method utilizes commercially available Nα-Fmoc amino acids for peptide synthesis and a new solid support. Three specific modifications of the solid-phase were made after the peptide and before the oligonucleotide assembly.
Unexpected preference of the E. coli translation system for the ester bond during incorporation of backbone-elongated substrates
Sando, Shinsuke,Abe, Kenji,Sato, Nobuhiko,Shibata, Toshihiro,Mizusawa, Keigo,Aoyama, Yasuhiro
, p. 6180 - 6186 (2008/02/03)
There have been recent advances in the ribosomal synthesis of various molecules composed of nonnatural ribosomal substrates. However, the ribosome has strict limitations on substrates with elongated backbones. Here, we show an unexpected loophole in the E. coli translation system, based on a remarkable disparity in its selectivity for β-amino/hydroxy acids. We challenged β-hydroxypropionic acid (β-HPA), which is less nucleophilic than β-amino acids but free from protonation, to produce a new repertoire of ribosome-compatible but main-chain-elongated substrates. PAGE analysis and mass-coupled S-tag assays of amber suppression experiments using yeast suppressor tRNAPheCUA confirmed the actual incorporation of β-HPA into proteins/oligopeptides. We investigated the side-chain effects of β-HPA and found that the side chain at position α and R stereochemistry of the β-substrate is preferred and even notably enhances the efficiency of incorporation as compared to the parent substrate. These results indicate that the E. coli translation machinery can utilize main-chain-elongated substrates if the pKa of the substrate is appropriately chosen.
