Elastin-like polypeptides are biotechnological protein and peptide carriers that offer a vast scope of applicability. This work aims to build a model for the expression of antimicrobial peptides by genetically engineering the Human Elastin-like Polypeptide platform developed in our lab. The well-characterized antimicrobial peptide indolicidin is selected as an example of antimicrobial domain for the recombinant fusion at the C-terminus of the carrier. The fusion construct has been designed to allow the release of the antimicrobial domain. The expression product has been purified and its physicochemical and antimicrobial properties has been characterized. Taking advantage of the self-assembling and matrix-forming properties of the recombinant biopolymer, the materials that are obtained have been evaluated for the antimicrobial activity toward bacterial-strain models. Our approach represents a cost-effective strategy for the production of smart components and materials endowed with antimicrobial capacity triggered by external stimuli.
