Inspired in naturally occurring fibrous proteins and composed of amino acid building blocks commonly found in structural proteins, protein-based polymers (PBPs) are a group of materials with unique chemical, physical and biological properties. Coventional recombinant DNA technology allows the biological synthesis of recombinant protein-based polymers (rPBPs) with precise control over its size and composition and the incorporation of functional bioactive domains such as antimicrobial peptides (AMPs). Owing to the unique balance between their mechanical properties, biocompatibility, biodegradability and thermostability, elastin-like recombinamers (ELRs) and silk-elastin like proteins (SELPs) are two of the most remarkable families of rPBP for biotechnological applications. Here, we describe the functionalization of a SELP and an ELR with different antimicrobial peptides that showed promising results against several Gram-positive and Gram-negative bacterial strains. This will provide the basis for the development of advanced biomaterials processed into different types of structures (e.g. hydrogels, films, fibers, particles) suitable for biomedical applications
