Optimization of the hydroxylamine cleavage of an expressed fusion protein to produce a recombinant antimicrobial peptide
Hydroxylamine was used to cleave the Asn-Gly peptide bond between the fusion partner and the antimicrobial peptide of interest, a magainin derivative (MSI-344). The efficiency of reaction depended on the hydroxylamine concentration, denaturant, pH, and the fused protein concentration. The optimal cleavage solution consisted of guanidine ⋅ HCl as the denaturant, pH 8.1, and 6.7 mg ml−1 of fuse
