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The lipopeptides pseudofactin II and surfactin effectively decrease Candida albicans adhesion and hydrophobicity. | LitMetric

The lipopeptides pseudofactin II and surfactin effectively decrease Candida albicans adhesion and hydrophobicity.

Antonie Van Leeuwenhoek

Faculty of Biotechnology, University of Wrocław, ul. Fryderyka Joliot-Curie 14a, 50-383, Wrocław, Poland.

Published: August 2015

A serious problem for humans is the propensity of Candida albicans to adhere to various surfaces and its ability to form biofilms. Surfactants or biosurfactants can affect the cell surfaces of microorganisms and block their adhesion to different substrates. This study investigated adhesion of C. albicans strains differing in cell surface hydrophobicity (CSH) to polystyrene microplates in order to compare the ability of lipopeptide biosurfactants pseudofactin (PF II) and surfactin (SU) to prevent fungal adhesion to polystyrene. The biosurfactants decreased adhesion of tested strains by 35-90 % when microplates were conditioned before the addition of cells. A 80-90 % reduction of adhesion was observed when cells were incubated together with lipopeptides in microplates. When microplates were pre-coated with biosurfactants, PF II was less active than SU, but when cells were incubated together with biosurfactants, the activity of both compounds was similar, independent of the CSH of strains. When cells were preincubated with lipopeptides and then the compounds were washed out, the adhesion of hydrophobic strains increased two times in comparison to control samples. This suggests irreversible changes in the cell wall after the treatment with biosurfactants. CSH of hydrophobic strains decreased only by 20-60 % after incubation with biosurfactants while adhesion decreased by 80-90 %; the changes in cell adhesion can be thus only partially explained through the modification of CSH. Preincubation of C. albicans with biosurfactants caused extraction of cell wall proteins with molecular mass in the range of 10-40 kDa, which is one possible mechanism of action of the tested lipopeptides.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4491367PMC
http://dx.doi.org/10.1007/s10482-015-0486-3DOI Listing

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