Comparison of the activity of two elastin-like recombinant carriers fused to the antimicrobial peptide indolicidin

Recombinant fusion biotechnology is a powerful tool for producing antimicrobial peptides (AMPs), which can contribute to limiting the number of potentially infectious microorganisms. AMPs are often expressed in fusion with a carrier protein, a strategy that prevents toxic effects on host bacterial cells and protects them from proteolytic degradation. Among the many fusion carriers available, elastin-like polypeptides offer several valuable advantages related to their unique thermo-responsive behavior. The Human Elastin-like Polypeptide was successfully employed to produce a model fusion construct with the indolicidin domain. Recently, an elastin-based variant of this polypeptide was developed, modulating the sequence of the hydrophobic domains, thus enhancing the phase transition properties. Here, a new carrier based on this sequence that was produced, physicochemically characterized, and employed as a fusion partner for the indolicidin is described. This work aims to compare two different elastin-based carriers and their indolicidin fusion derivatives, as well as to determine, based on their properties, which may be the most advantageous carrier for producing antimicrobial domains. This study was focused on the elastin-like polypeptides as a tunable expression platform particularly suitable for producing AMPs and for their integration in biomimetic interfaces that acquire the capacity to inhibit bacterial growth.