Unravelling the Structural and Molecular Basis Responsible for the Anti-Biofilm Activity of Zosteric Acid

PLoS One. 2015 Jul 1;10(7):e0131519. doi: 10.1371/journal.pone.0131519. eCollection 2015.

Abstract

The natural compound zosteric acid, or p-(sulfoxy)cinnamic acid (ZA), is proposed as an alternative biocide-free agent suitable for preventive or integrative anti-biofilm approaches. Despite its potential, the lack of information concerning the structural and molecular mechanism of action involved in its anti-biofilm activity has limited efforts to generate more potent anti-biofilm strategies. In this study a 43-member library of small molecules based on ZA scaffold diversity was designed and screened against Escherichia coli to understand the structural requirements necessary for biofilm inhibition at sub-lethal concentrations. Considerations concerning the relationship between structure and anti-biofilm activity revealed that i) the para-sulfoxy ester group is not needed to exploit the anti-biofilm activity of the molecule, it is the cinnamic acid scaffold that is responsible for anti-biofilm performance; ii) the anti-biofilm activity of ZA derivatives depends on the presence of a carboxylate anion and, consequently, on its hydrogen-donating ability; iii) the conjugated aromatic system is instrumental to the anti-biofilm activities of ZA and its analogues. Using a protein pull-down approach, combined with mass spectrometry, the herein-defined active structure of ZA was matrix-immobilized, and was proved to interact with the E. coli NADH:quinone reductase, WrbA, suggesting a possible role of this protein in the biofilm formation process.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anions
  • Anti-Bacterial Agents / chemical synthesis
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology*
  • Biofilms / drug effects*
  • Biofilms / growth & development
  • Carboxylic Acids / chemistry
  • Cinnamates / chemical synthesis
  • Cinnamates / chemistry
  • Cinnamates / pharmacology*
  • Escherichia coli / drug effects*
  • Escherichia coli / enzymology
  • Escherichia coli / growth & development
  • Escherichia coli Proteins / antagonists & inhibitors*
  • Escherichia coli Proteins / chemistry
  • Hydrogen / chemistry
  • Microbial Sensitivity Tests
  • Microbial Viability / drug effects
  • Protein Binding
  • Repressor Proteins / antagonists & inhibitors*
  • Repressor Proteins / chemistry
  • Small Molecule Libraries / chemical synthesis
  • Small Molecule Libraries / chemistry
  • Small Molecule Libraries / pharmacology*
  • Structure-Activity Relationship
  • Sulfuric Acid Esters / chemical synthesis
  • Sulfuric Acid Esters / chemistry
  • Sulfuric Acid Esters / pharmacology*

Substances

  • Anions
  • Anti-Bacterial Agents
  • Carboxylic Acids
  • Cinnamates
  • Escherichia coli Proteins
  • Repressor Proteins
  • Small Molecule Libraries
  • Sulfuric Acid Esters
  • WrbA protein, E coli
  • zosteric acid
  • Hydrogen

Grants and funding

This work was supported by Fondazione Cariplo, grant n. 2011-0277 (FC). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.