Synergetic Antifouling and Antimicrobial Activity by Simple Peptide Particles

Biofouling is an undesirable process in which organisms and their by-products encrust a surface. Antifouling solutions are of great importance since biofouling has negative effects on numerous species, ecosystems, and areas including water treatment facilities, health-care systems, and marine devices. We describe the self-assembly of a tripeptide into well-ordered structures that can act as antifouling agents, and together with glucose oxidase, can also exhibit antibacterial activity. The peptide self-assembles into two different types of supramolecular structures, depending on the pH of the solution. When applied on bare glass, these structures change the physical and chemical fatures of the surface and provide the surfaces with antifouling activity. We present the dynamics simulations of the self-assembly process and suggest a mechanism for the antifouling based on these findings.

In addition, these assemblies can adsorb and release active compounds. We demonstrate the mechanisms of association of an aticancer drug, antibiotic and an enzyme with these structures. Importantly, we showed that the catalytic activity of the enzyme Glucose Oxidase which results in the formation of hydrogen peroxide, synergistically act as an antimicrobial agent with the antifouling properties of the peptide. This combined activity is very important for developing new sterile surfaces. These surfaces can be useful in health-care systems for preventing bacterial contamination, in water purification devices, food packaging surfaces, and any other environment that suffers from bacterial contamination.