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 (AMPs) by genetically engineering the Human Elastin-like Polypeptide platform developed in the lab. The well-characterized AMP indolicidin is selected as an example of an 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 antimicrobial activity toward bacterial-strain models. This approach represents a cost-effective strategy for the production of smart components and materials endowed with antimicrobial capacity triggered by external stimuli.
Keywords: antimicrobial peptides; hydrogel matrix; recombinant biopolymers; smart materials.
© 2023 The Authors. Macromolecular Bioscience published by Wiley-VCH GmbH.