Production of bioactive hepcidin by recombinant DNA tagging with an elastin-like recombinamer

Abstract

With the lack of new chemical antibiotics and the increasing pathogen resistance to those available, new alternatives are being explored. Antimicrobial peptides (AMPs) with a broad range of effects such as antibacterial, antifungal, and antiviral, arise as one of the options. These can be produced by recombinant DNA technology however, the chromatographic methods used for peptide purification are costly and time consuming. Here, we describe the design, production, purification and assessment of the antibacterial activity of the human peptide Hepcidin, using an elastin-like recombinamer as fusion partner. The recombinant protein Hep-A200 was produced in Escherichia coli and purified by a non-chromatographic procedure, exploiting the thermal properties of A200 elastin-like recombinamer. The recombinant polymer Hep-A200 retained antibacterial activity against Gram-positive and Gram-negative species.