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Impact of Aluminum on the Oxidation of Lipids and Enzymatic Lipolysis in Monomolecular Films at the Air/Water Interface

Year: 2007

Journal: Langmuir, 2007, 23 (6), pp 3338–3348, 20111221

Authors: Yohann Corvis, Beata Korchowiec, Gerald Brezesinski, Sébastien Follot, and Ewa Rogalska

Organizations: Nancy 1, Faculté des Sciences, BP 239, 54506 Vandoeuvre-lés-Nancy cedex, France, Department of Physical Chemistry and Electrochemistry, Faculty of Chemistry, Jagiellonian University, ul. Romana Ingardena 3, 30-060 Krakow, Poland, and Max Planck Institute of Colloids and Interfaces, Research Campus Golm, Am Mühlenberg 1, 14476 Potsdam, Germany

There is evidence that serious pathologies are associated with aluminum (Al). In the present work, the influence of Al on enzymatic lipolysis was studied with the aim to get more insight into the possible link between the Al-induced membrane modification and the cytotoxicity of the trivalent cation (AlIII). Lipid monolayers were used as model membranes. The monomolecular film technique allowed monitoring the Al-dependent modifications of the lipid monolayer properties and enzyme kinetics. Two enzymes, namely, Candida rugosa lipase and a calcium (CaII)-dependent phospholipase A2 from porcine pancreas, were used to catalyze the lipolysis of triglyceride and phosphoglyceride monolayers, respectively. The results obtained show that Al modifies both the monolayer structure and enzymatic reaction rates. While the enzymes used in this study can be considered as probes detecting lipid membrane properties, it cannot be excluded that in physiological conditions modulation of the enzyme action by the Al-bound membranes is among the reasons for Al toxicity.