A Ti6Al4V functionalized with a quorum quenching enzyme and biocompatible in a Caenorhabditis elegans model system

Implant-associated infections, particularly periprosthetic joint infections, together with the rise of antibiotic-resistant pathogens such as Pseudomonas aeruginosa, highlight the need for alternative anti-infective strategies. In this study, we developed a functionalized Ti6Al4V surface based on the immobilization of a quorum-quenching lactonase enzyme (ST1-YtnP) to disrupt bacterial communication and biofilm formation. The surface modification involved chemical etching, calcium incorporation, and enzyme immobilization. Successful functionalization was confirmed by surface charge analysis and compositional characterization, indicating changes consistent with enzyme grafting, along with increased surface hydrophilicity. Biocompatibility was evaluated in vivo using a Caenorhabditis elegans model, demonstrating that the functionalized surfaces are non-toxic. Importantly, the potential toxicity associated with glycerol present in the enzyme solution was eliminated upon enzyme immobilization. Overall, these results demonstrate that ST1-YtnP-functionalized Ti6Al4V represents a promising strategy for the development of antivirulence biomaterial surfaces, offering an approach to reduce infection risk without contributing to antibiotic resistance