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Updated: Jan 27, 2026

Analysis of Histone Antibody Specificity with Peptide Microarrays
Published on: August 1, 2017
Reprogramming Promiscuous Nonribosomal Peptide Synthetases for Production of Specific Peptides
Xiaofeng Cai1,2, Lei Zhao1, Helge B Bode1,3
1Molecular Biotechnology, Department of Biosciences , Goethe University Frankfurt , 60438 Frankfurt am Main , Germany.
Abstract:
Pairs of docking domains (DDs) mediate the selective interations between adjacent nonribosomal peptide synthetases (NRPSs) to form defined protein-protein interactions resulting in defined peptide sequences. New specific rhabdopeptide/xenortide-like peptides (RXPs) were generated by swapping of either flexible or nonfunctional DD pairs between these monomodular RXP-NRPSs against DDs from collinear NRPSs. The results presented a promising means of engineering RXP-producing NRPSs to obtain desired peptides and further substantiated the decisive role of DDs in the NRP synthesis.
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