Antibiofilm surfaces based on the immobilization of a novel recombinant antimicrobial multidomain protein using self-assembled monolayers

Abstract

The constant increase of microorganisms resistant to antibiotics has been classified as a global health emergency, which is especially challenging when biofilms are formed. Herein, novel biofunctionalized gold surfaces with the antimicrobial multidomain recombinant protein JAMF1, both in the soluble form and nanostructured as nanoparticles, were developed. The interaction between His-tag termination of the protein and a nitriloacetic acid–Ni complex formed on mixed self-assembled monolayers (mixed SAMs) was exploited. The obtained antibiofilm surfaces based on the immobilization of the novel JAMF1 protein using self-assembled monolayers were characterized using a multi-technique approach including: cyclic voltammetry, X-ray photoelectron spectroscopy, atomic force microscopy and fluorescence, proving that the modification and immobilization of JAMF1 were successfully done. The antibiofilm activity against Escherichia coli and carbapenem-resistant Klebsiella pneumoniae showed that the immobilized antimicrobial proteins were able to reduce biofilm formation of both microorganisms. This strategy opens up new possibilities for controlled biomolecule immobilization for fundamental biological studies and biotechnological applications, at the interface of materials science and molecular biology.