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dc.contributor.author
Lopes, José Luiz S.
dc.contributor.author
Nobre, Thatyane M.
dc.contributor.author
Siano, Alvaro Sebastían
dc.contributor.author
Humpola, Verónica
dc.contributor.author
Bossolan, Nelma R.S.
dc.contributor.author
Zaniquelli, Maria. E.D.
dc.contributor.author
Tonarelli, Georgina Guadalupe
dc.contributor.author
Beltramini, Leila M.
dc.date.available
2020-04-06T13:51:46Z
dc.date.issued
2009-10
dc.identifier.citation
Lopes, José Luiz S.; Nobre, Thatyane M.; Siano, Alvaro Sebastían; Humpola, Verónica; Bossolan, Nelma R.S.; et al.; Disruption of Saccharomyces cerevisiae by Plantaricin 149 and investigation of its mechanism of action with biomembrane model systems; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1788; 10; 10-2009; 2252-2258
dc.identifier.issn
0005-2736
dc.identifier.uri
http://hdl.handle.net/11336/102016
dc.description.abstract
The action of a synthetic antimicrobial peptide analog of Plantaricin 149 (Pln149a) against Saccharomyces 24 ^ cerevisiae and its interaction with biomembrane model systems were investigated. Pln149a was shown to 25 inhibit S. cerevisiae growth by more than 80% in YPD medium, causing morphological changes in the yeast 26 wall and remaining active and resistant to the yeast proteases even after 24 h of incubation. Different 27 membrane model systems and carbohydrates were employed to better describe the Pln149a interaction with 28 cellular components using circular dichroism and fluorescence spectroscopies, adsorption kinetics and 29 surface elasticity in Langmuir monolayers. These assays showed that Pln149a does not interact with either 30 mono/polysaccharides or zwitterionic LUVs, but is strongly adsorbed to and incorporated into negatively 31 charged surfaces, causing a conformational change in its secondary structure from random-coil to helix upon 32 adsorption. From the concurrent analysis of Pln149a adsorption kinetics and dilatational surface elasticity 33 data, we determined that 2.5 μM is the critical concentration at which Pln149a will disrupt a negative DPPG 34 monolayer. Furthermore, Pln149a exhibited a carpet-like mechanism of action, in which the peptide initially 35 binds to the membrane, covering its surface and acquiring a helical structure that remains associated to the 36 negatively charged phospholipids. After this electrostatic interaction, another peptide region causes a strain 37 in the membrane, promoting its disruption.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
antimicrobial peptides
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Mechanism of antimicrobial activity
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Peptide-lipid interaction
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Saccharomyces cerevisiae inhibition
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Otras Ciencias Químicas
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Disruption of Saccharomyces cerevisiae by Plantaricin 149 and investigation of its mechanism of action with biomembrane model systems
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-04-02T13:22:45Z
dc.journal.volume
1788
dc.journal.number
10
dc.journal.pagination
2252-2258
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Lopes, José Luiz S.. Universidade de Sao Paulo; Brasil
dc.description.fil
Fil: Nobre, Thatyane M.. Universidade de Sao Paulo; Brasil
dc.description.fil
Fil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral; Argentina
dc.description.fil
Fil: Humpola, Verónica. Universidad Nacional del Litoral; Argentina
dc.description.fil
Fil: Bossolan, Nelma R.S.. Universidade de Sao Paulo; Brasil
dc.description.fil
Fil: Zaniquelli, Maria. E.D.. Universidade de Sao Paulo; Brasil
dc.description.fil
Fil: Tonarelli, Georgina Guadalupe. Universidad Nacional del Litoral; Argentina
dc.description.fil
Fil: Beltramini, Leila M.. Universidade de Sao Paulo; Brasil
dc.journal.title
Biochimica et Biophysica Acta - Biomembranes
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273609002260
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbamem.2009.06.026
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