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Issue 43, 2013
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Interaction of sphingomyelinase with sphingomyelin-containing supported membranes

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We have studied the interaction of the enzyme sphingomyelinase with sphingomyelin-containing supported membranes using quantitative applications of real-time epifluorescence microscopy and imaging optical ellipsometry. The enzymatic action converts sphingomyelin into ceramides by cleaving the phosphodiester bond. Our results confirm previous studies establishing a gross morphological transformation of lipid bilayers involving a multi-step process consisting of lag-burst type of enzyme activation and in-plane reorganization of membrane components attributed to the formation of ceramide-enriched domains. A unique finding of our study is the evidence for the existence of an additional out-of-plane deformation following lateral reorganization resulting in membrane voids disrupting the laterally contiguous bilayer. Taken together, the in-plane and out-of-plane deformations suggest a mechanistic picture in which lateral diffusional processes of translational mobility and phase separation couple with out-of-plane interactions across the membrane leaflet to induce irreversible membrane disruption in response to SMase action. Remarkably, lipid monolayers supported on hydrophobic substrates exhibit no such large-scale deformation despite ceramide generation by enzymatic activity of sphingomyelinase, possibly suggesting the importance of coupling across membrane leaflets in inducing out-of-plane deformations.

Graphical abstract: Interaction of sphingomyelinase with sphingomyelin-containing supported membranes

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Publication details

The article was received on 08 Jul 2013, accepted on 19 Sep 2013 and first published on 09 Oct 2013

Article type: Paper
DOI: 10.1039/C3SM51855H
Citation: Soft Matter, 2013,9, 10413-10420

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    Interaction of sphingomyelinase with sphingomyelin-containing supported membranes

    V. N. Ngassam, A. E. Oliver, P. N. Dang, E. L. Kendall, S. F. Gilmore and A. N. Parikh, Soft Matter, 2013, 9, 10413
    DOI: 10.1039/C3SM51855H

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