Bacterial biofilms represent an essential part of Earth’s ecosystem that can cause multiple ecological, technological and health problems. The environmental resilience and sophisticated organization of biofilms acting like a multicellular organism are enabled by the extracellular matrix (ECM) that creates a protective network of biomolecules around the bacterial community. Current anti-biofilm agents can interfere with ECM production but, being based on small molecules, they can be degraded by bacteria and rapidly diffuse away from biofilms. Both factors severely reduce their efficacy, while their toxicity to higher organisms create additional barriers to their practicality. In the past, we observed semi-selective self-assembly of inorganic nanoparticles (NPs) with a library of proteins that paved the way to their further experimental and computational studies. In this study, we report on the ability of graphene NPs (GNPs) to effectively disperse mature <i>Staphylococcus aureus</i> biofilms, interfering with the self-assembly of amyloid fibers - a key structural component of the ECM. Mimicking peptide-binding biomolecules, GNPs form supramolecular complexes with phenol soluble modulins (PSMs), the peptide monomers of amyloid fibers. Experimental and computational results show that GNPs efficiently dock near the <i>N</i>-terminus of the peptide and change the secondary structure of PSM, which disrupts their fibrillation and represents a novel strategy for mitigation of bacterial communities.

Self-assembly of biomimetic nanoparticles with amyloid proteins: Concept and functions

2019 Spring National Meeting

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