A novel method for post-treatment of gene-engineered proteins is reported.
A coden of Cys-His unit is introduced into the N-terminal of cecropin CMIV
by using PCR. The gene is expressed in E. coil fused with GST. After purifi
cation, the fusion protein is cleaved by [Pd(en)(H2O)(2)](2+) at the His-Ar
g bond and the cecropin CMIV with antibacterial activity is obtained. The p
reliminary results held some promise of success for application of the pall
adium(II) complex as cleavage agent for the production of peptide drugs fro
m gene-engineering fusion proteins.