Antimycotic activity of fengycin C biosurfactant and its interaction with phosphatidylcholine model membranes

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dc.citation.journalTitleCOLLOIDS AND SURFACES B-BIOINTERFACESspa
dc.contributor.authorGonzález-Jaramillo LM
dc.contributor.authorAranda FJ
dc.contributor.authorTeruel JA
dc.contributor.authorVillegas-Escobar V
dc.contributor.authorOrtiz A
dc.contributor.departmentUniversidad EAFIT. Departamento de Cienciasspa
dc.contributor.researchgroupCiencias Biológicas y Bioprocesos (CIBIOP)spa
dc.date.accessioned2021-03-23T20:09:00Z
dc.date.available2021-03-23T20:09:00Z
dc.date.issued2017-08-01
dc.description.abstractLipopeptide biosurfactants constitute one of the most promising groups of compounds for the treatment and prevention of fungal diseases in plants. Bacillus subtilis strain EA-CB0015 produces iturin A, fengycin C and surfactin and it has been proven useful for the treatment of black Sigatoka disease in banana plants, an important pathology caused by the fungus Mycosphaerella fijiensis (Morelet). We have found that B. subtilis EA-CB0015 cell free supernatants and purified fractions inhibit M. fijiensis cellular growth. The effect of the purified lipopeptides mentioned above on fungal growth has been also evaluated, observing that iturin A and fengycin C inhibit mycelial growth and ascospore germination, whereas surfactin is not effective. On the hypothesis that the antifungal action of the lipopeptides is associated to their incorporation into biological membranes, ultimately leading to membrane permeabilization, a detailed biophysical study on the interaction of a new isoform of fengycin C with model dipalmitoyphosphatidylcholine (DPPC) membranes has been carried out. Differential scanning calorimetry shows that fengycin C alters the thermotropic phase transitions of DPPC, and is laterally segregated in the fluid bilayer forming domains. Fluorescent probe polarization measurements show that fengycin C does not affect the hydrophobic interior of the membrane. This latter perturbation is concomitant with a strong dehydration of the polar region of DPPC, as shown by FTIR. Fengycin-rich domains, where the surrounding DPPC molecules are highly dehydrated, may well constitute sites of membrane permeabilization leading to a leaky target membrane. These results are a solid support to explain the membrane perturbing action of fengycin, which has been related to its antifungal activity. (C) 2017 Elsevier B.V. All rights reserved.eng
dc.identifierhttps://eafit.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=6639
dc.identifier.doi10.1016/j.colsurfb.2017.05.021spa
dc.identifier.issn09277765spa
dc.identifier.issn18734367spa
dc.identifier.otherWOS;000445982100006
dc.identifier.otherSCOPUS;2-s2.0-85050518863
dc.identifier.urihttp://hdl.handle.net/10784/26826
dc.language.isoengeng
dc.publisherELSEVIER SCIENCE BV
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85019548465&doi=10.1016%2fj.colsurfb.2017.05.021&partnerID=40&md5=e5d6df9f7ca5a1a2eea2c06af93a174d
dc.rightshttps://v2.sherpa.ac.uk/id/publication/issn/0927-7765
dc.sourceCOLLOIDS AND SURFACES B-BIOINTERFACES
dc.subject.keywordFengycin biosurfactanteng
dc.subject.keywordBacillus subtiliseng
dc.subject.keywordMycosphaerella fijiensiseng
dc.subject.keywordPhospholipid model membraneseng
dc.subject.keywordDifferential scanning calorimetryeng
dc.subject.keywordFTIReng
dc.titleAntimycotic activity of fengycin C biosurfactant and its interaction with phosphatidylcholine model membraneseng
dc.typearticleeng
dc.typeinfo:eu-repo/semantics/articleeng
dc.typeinfo:eu-repo/semantics/publishedVersioneng
dc.typepublishedVersioneng
dc.type.localArtículo

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