Development of a peptide resistant to proteolysis followed by synthesis of a plasmid encoding its sequence for expression in a biological object

Studies have been conducted on the construction of a bioactive proteolysis-resistant peptide sequence of the CDF-11 protein followed by the synthesis of a plasmid encoding its expression in E.coli. The prediction of biological activity, resistance to proteolysis and bioavailability of the peptide sequence was carried out on the ADMET platform. The synthesis of plasmids of the peptide sequence of a new recombinant protein was carried out in the Russian biotechnology company “Eurogen” (Moscow) by cyclic assembly of oligonucleotides. The molecular weight distribution of the peptide sequence was evaluated by mass spectrometry. The peptide sequence was identified by the MALDI-TOF MS Ultraflex method. The peptide sequence of the GDF-11 LQIIYGKIPR protein was cyclized by introducing and crosslinking three cysteine residues and a new LQIIYGKIPR sequence was obtained. The predicted values of the bioavailability and clinical use of the new peptide indicate the effectiveness of its proposed modification and the possibility of oral administration. For the expression of a recombinant protein with increased stability to proteolysis and bioavailability containing a cyclic peptide sequence, a plasmid was obtained and synthesized, and the sequence of amino acids in it was determined. Further research will focus on the expression of the modified GDF 11 mut protein in E.coli.