Albumin biofunctionalization to minimize the Staphylococcus aureus adhesion on solid substrates. Academic Article uri icon

Overview

abstract

  • Staphylococcus aureus has become the most common opportunistic microorganism related to nosocomial infections due to the bacteria capacity to form biofilms on biomedical devices and implants. Since bacterial adhesion is the first step in this pathogenesis, it is evident that inhibiting such a process will reduce the opportunity for bacterial colonization on the devices. This work is aimed at optimizing a surface biofunctionalization strategy to inhibit the adhesion of S. aureus on solid substrates. The first part of the work deals with the albumin adsorption-desorption process, studied by a factorial design of experiments to explore a wide range of experimental factors (protein concentration, pH, flow rate and adsorption time) and responses (initial adsorption rate, adsorbed amount, desorbed extent) for hydrophilic and hydrophobic substrates, with a reduced number of experiments. This approach allows the simultaneous evaluation of the factors affecting the albumin adsorption-desorption process to find a qualitative correlation with the amount of alive S. aureus adhered on albumin biofunctionalized substrates. The results of this work point to a relationship between bacterial adhesion and the degree of albumin relaxation on the solid substrate. In fact, the inhibition of bacterial adhesion on albumin biofunctionalized substrates is due to the surface perturbation on the native structure of the protein. On this base, a biofunctionalization strategy was designed using a solution of thermally treated albumin molecules (higher β-sheet or unordered secondary structure elements) to biofunctionalize solid substrates by dipping. With these albumin biofunctionalized substrates S. aureus adhesion was minimized.

publication date

  • April 3, 2018

Research

keywords

  • Bacterial Adhesion
  • Serum Albumin
  • Serum Albumin, Bovine
  • Staphylococcus aureus

Identity

Scopus Document Identifier

  • 85045052099

Digital Object Identifier (DOI)

  • 10.1016/j.colsurfb.2018.04.006

PubMed ID

  • 29649785

Additional Document Info

volume

  • 167