Blistering of supported lipid membranes induced by Phospholipase D, as observed by real-time atomic force microscopy

10Citations
Citations of this article
22Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

Phospholipase D from Streptomyces chromofuscus (PLDSc) is a soluble enzyme known to be activated by the phosphatidic acid (PA)-calcium complexes. Despite the vast body of literature that has accumulated on this enzyme, the exact mechanism of activation remains poorly understood. In this work, we report the first observation of PLDSc activity in real time and at nanometer resolution using atomic force microscopy (AFM). AFM images of continuous and patchy dipalmitoylphosphatidylcholine (DPPC) bilayers were recorded, prior and after incubation with PLDSc. For continuous bilayers, the enzyme induced important morphological alterations; holes corresponding to the bilayer thickness were created, while an additional elevated phase, about 2.5 nm high, was observed. This bilayer blistering is believed to be due to the production of the negatively charged lipid PA that would cause localized repulsions between the bilayer and the underlying mica surface. By contrast, these elevated domains were not seen on patchy bilayers incubated with the enzyme. Instead, the shapes of DPPC patches were strongly deformed by enzyme activity and evolved into melted morphologies. These results point to the importance of lipid packing on PLD activity and illustrate the potential of AFM for visualizing remodeling enzymatic activities. © 2007 Elsevier B.V. All rights reserved.

Cite

CITATION STYLE

APA

El Kirat, K., Duprès, V., & Dufrêne, Y. F. (2008). Blistering of supported lipid membranes induced by Phospholipase D, as observed by real-time atomic force microscopy. Biochimica et Biophysica Acta - Biomembranes, 1778(1), 276–282. https://doi.org/10.1016/j.bbamem.2007.09.029

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free