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    Action of Vipoxin and its separated components on monomolecular film of Dilauroylphosphatidylcholine at the air/water interface

    Year: 2019

    Journal: Colloid Surf. A-Physicochem. Eng. Asp., Volume 562, 1-Feb, page 196–202

    Authors: Mircheva, K.; Petrova, S. D.; Ivanova, Tz.; Panaiotov, I.; Balashev, K. T.

    Organizations: Horizon 2020 project [692146-H2020-eu.4.b]; Fulbright grant [18-21-05]

    Keywords: Phospholipases A(2); Vipoxin; Atomic force microscopy (AFM); Enzyme kinetics

    The growing research interest about neurotoxin Vipoxin is inspired by its intriguing heterodimeric structure and the resulting interactions between Vipoxin's basic catalytic subunit and the acidic regulatory subunit. In this paper we studied the enzymatic action of Vipoxin and its individual components on Dilauroylphosphatidylcholine (DLPC) monolayers at air-water interfaces. We applied the classical surface barostatic method and interpreted our experimental data with an adapted Michaelis-Menten kinetic model. This approach allowed us to obtain the global kinetic constants together with the interfacial specific activity of Vipoxin and its subunits. Using reconstituted Vipoxin complexes formed by incubating the enzymatic VBC-sPLA(2) and non-catalytic VAC subunits in different ratios, we showed that the activity of the reconstituted mixture VAC:VBC-sPLA(2) (1:1), which should correspond to the composition of Vipoxin, is higher than that of the natural Vipoxin complex. Finally, Vipoxin heterodimers in the DLPC monolayer were imaged by Atomic force microscope (AFM) and statistically analyzed.
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