Unravelling the structural and molecular basis responsible for the anti-biofilm activity of zosteric acid

dc.contributor.authorCatto, C.
dc.contributor.authorDell'Orto, S.
dc.contributor.authorVilla, Federica
dc.contributor.authorVilla, S.
dc.contributor.authorGelain, A.
dc.contributor.authorVitali, A.
dc.contributor.authorMarzano, V.
dc.contributor.authorBaroni, S.
dc.contributor.authorForlani, F.
dc.date.accessioned2016-11-14T23:47:30Z
dc.date.available2016-11-14T23:47:30Z
dc.date.issued2015-07
dc.description.abstractThe 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.en_US
dc.identifier.citationCattò C, Dell’Orto S, Villa F, Villa S, Gelain A, Vitali A, Marzano V, Baroni S, Forlani F, ʺUnravelling the structural and molecular basis responsible for the anti-biofilm activity of zosteric acid,ʺ PLoS ONE 2015 10(7): e0131519en_US
dc.identifier.issn1932-6203
dc.identifier.urihttps://scholarworks.montana.edu/handle/1/11505
dc.rightsCC BY 4.0en_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/legalcodeen_US
dc.titleUnravelling the structural and molecular basis responsible for the anti-biofilm activity of zosteric aciden_US
dc.typeArticleen_US
mus.citation.extentfirstpagee0131519en_US
mus.citation.issue7en_US
mus.citation.journaltitlePLoS ONEen_US
mus.citation.volume10en_US
mus.data.thumbpage5en_US
mus.identifier.categoryChemical & Material Sciencesen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1371/journal.pone.0131519en_US
mus.relation.collegeCollege of Engineeringen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentBiological Sciences.en_US
mus.relation.departmentCenter for Biofilm Engineering.en_US
mus.relation.departmentChemical & Biological Engineering.en_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.researchgroupCenter for Biofilm Engineering.en_US
mus.relation.universityMontana State University - Bozemanen_US

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