A novel technique for the effective production of short peptide analogs from concatameric short peptide multimers

We designed a basic unit of the modified chicken gonadotropin releasing hor mone II (cGnRH-II) peptide containing a trypsin cleavable linker peptide at both ends of the original peptide. We made a synthetic DNA coding for the modified cGnRH-II peptide with asymmetric and complementary cohesive ends o f linker nucleotides. A tandemly repeated DNA cassette for the expression o f concatameric short peptide multimers was constructed by ligating the basi c units. The expressed peptide multimers mere purified and subject to amino -terminal sequence analysis, which displayed the amino acid sequences expec ted from the designed nucleotides of the expression cassette. The monomeric cGnRH-II peptide analogs were generated after trypsin digestion. The prese nt results showed that the technique developed for the production of the co ncatameric peptide multimers with cleavable tinker peptides can be generall y applicable to the production of short peptide analogs.