Unravelling the structural and molecular basis responsible for the anti-biofilm activity of zosteric acid
dc.contributor.author | Catto, C. | |
dc.contributor.author | Dell'Orto, S. | |
dc.contributor.author | Villa, Federica | |
dc.contributor.author | Villa, S. | |
dc.contributor.author | Gelain, A. | |
dc.contributor.author | Vitali, A. | |
dc.contributor.author | Marzano, V. | |
dc.contributor.author | Baroni, S. | |
dc.contributor.author | Forlani, F. | |
dc.date.accessioned | 2016-11-14T23:47:30Z | |
dc.date.available | 2016-11-14T23:47:30Z | |
dc.date.issued | 2015-07 | |
dc.description.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. | en_US |
dc.identifier.citation | Cattò 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): e0131519 | en_US |
dc.identifier.issn | 1932-6203 | |
dc.identifier.uri | https://scholarworks.montana.edu/handle/1/11505 | |
dc.rights | CC BY 4.0 | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/legalcode | en_US |
dc.title | Unravelling the structural and molecular basis responsible for the anti-biofilm activity of zosteric acid | en_US |
dc.type | Article | en_US |
mus.citation.extentfirstpage | e0131519 | en_US |
mus.citation.issue | 7 | en_US |
mus.citation.journaltitle | PLoS ONE | en_US |
mus.citation.volume | 10 | en_US |
mus.data.thumbpage | 5 | en_US |
mus.identifier.category | Chemical & Material Sciences | en_US |
mus.identifier.category | Life Sciences & Earth Sciences | en_US |
mus.identifier.doi | 10.1371/journal.pone.0131519 | en_US |
mus.relation.college | College of Engineering | en_US |
mus.relation.college | College of Letters & Science | en_US |
mus.relation.department | Biological Sciences. | en_US |
mus.relation.department | Center for Biofilm Engineering. | en_US |
mus.relation.department | Chemical & Biological Engineering. | en_US |
mus.relation.department | Microbiology & Immunology. | en_US |
mus.relation.researchgroup | Center for Biofilm Engineering. | en_US |
mus.relation.university | Montana State University - Bozeman | en_US |
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