A simple surface biofunctionalization strategy to inhibit the biofilm formation by Staphylococcus aureus on solid substrates. Academic Article uri icon

Overview

abstract

  • Staphylococcus aureus is an important opportunistic pathogen that causes a broad range of infections due to the bacteria capacity to form biofilms on medical devices. This work is aimed at inhibiting the biofilm formation by S. aureus on solid substrates using a simple surface biofunctionalization strategy. We previously found that surface biofunctionalization with structural perturbed albumin inhibited the initial stage of S. aureus adhesion. The current work extends this strategy with other plasma protein, fibrinogen, which in addition can be bond specifically to the cell wall-anchored proteins of S. aureus. The study of fibrinogen adsorption indicates that the fraction of surface-perturbed molecules is enlarged at long adsorption times and low protein concentration. In these conditions, a significant diminution of ca.60% of alive adhered bacteria were observed after 40 min and the biofilm formation was completely prevented. Thus, it seems that the inhibition of bacterial adhesion on substrates with surface-perturbed proteins represents a general trend even when specific interactions are present. On this basis, we developed a simple strategy to inhibit the formation of S. aureus biofilm, using thermally treated albumin or fibrinogen molecules prior to the substrate biofunctionalization. This strategy shows an excellent performance since the alive adhered bacteria diminishes ca. 90% at short incubation time, followed by the fully inhibition of biofilm formation. This novel and simple resource represents a change of the usual notion in avoiding post-surgery infections, mostly related to the use of medical devices.

publication date

  • August 7, 2019

Research

keywords

  • Bacterial Adhesion
  • Biofilms
  • Cell Wall
  • Fibrinogen
  • Staphylococcus aureus

Identity

Scopus Document Identifier

  • 85070584984

Digital Object Identifier (DOI)

  • 10.1016/j.colsurfb.2019.110432

PubMed ID

  • 31421403

Additional Document Info

volume

  • 183