| abstract |
It has become clear that if a peptide having a thiol group near an amino group, and having, at the N-terminal, an amino acid residue, which introduced a specific protective group into the thiol group and amino group, undergoes translation by initiation suppression, the likelihood of an amino acid translation reaction being initiated will increase. Moreover, cleaved peptide generation will be suppressed, improving the translation efficiency and purity. Also, it has become clear that it is possible to efficiently promote a cyclisation reaction in the peptide due to an amide bond. Based on these findings, a new method for producing a peptide and nucleic acid complex, the peptide containing numerous unnatural amino acids and having a site for cyclisation due to an amide bond, was found. |