Nanosilver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition

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DOI

  • Zil-E Huma, Monash University, Lahore University of Management Sciences
  • ,
  • Ibrahim Javed, Monash University, The University of Queensland
  • ,
  • Zhenzhen Zhang, Clemson University
  • ,
  • Hajira Bilal, Monash University
  • ,
  • Yunxiang Sun, Clemson University, Ningbo University
  • ,
  • Syed Zajif Hussain, Lahore University of Management Sciences
  • ,
  • Thomas P Davis, Monash University, The University of Queensland
  • ,
  • Daniel E Otzen
  • Cornelia B Landersdorfer, Monash University
  • ,
  • Feng Ding, Clemson University
  • ,
  • Irshad Hussain, Lahore University of Management Sciences
  • ,
  • Pu Chun Ke, Monash University

Multidrug resistance of bacteria is a major challenge due to the wide-spread use of antibiotics. While a range of strategies have been developed in recent years, suppression of bacterial activity and virulence via their network of extracellular amyloid has rarely been explored, especially with nanomaterials. Here, silver nanoparticles and nanoclusters (AgNPs and AgNCs) capped with cationic branched polyethylenimine polymer are synthesized, and their antimicrobial potentials are determined at concentrations safe to mammalian cells. Compared with the ultrasmall AgNCs, AgNPs entail stronger binding to suppress the fibrillization of FapC, a major protein constituent of the extracellular amyloid matrix of Pseudomonas aeruginosa. Both types of nanoparticles exhibit concentration-dependent antibiofilm and antimicrobial properties against P. aeruginosa. At concentrations of 1 × 10-6 m or below, both the bactericidal activity of AgNCs and the antibiofilm capacity of AgNPs are associated with their structure-mediated bio-nano interactions but not ion release. For AgNPs, specifically, their antibiofilm potency correlates with their capacity of FapC fibrillization inhibition, but not with their bactericidal activity. This study demonstrates the antimicrobial potential of safe nanotechnology through the novel route of amyloidosis inhibition.

OriginalsprogEngelsk
Artikelnummer1906674
TidsskriftSmall (Weinheim an der Bergstrasse, Germany)
Vol/bind16
Nummer21
Antal sider10
ISSN1613-6810
DOI
StatusUdgivet - maj 2020

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