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.
