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Poster De Conférence Année : 2012

The bulk association mechanism between lysozyme and α-lactalbumine is revealed by interfacial measurements

Résumé

Controlled interactions and assembly of proteins with one another promise to be a powerful approach for generating novel supramolecular architectures. In this study, we report on two oppositely charged proteins, Lysozyme (LYS) and alpha-Lactalbumine (ALA) which self-assemble into well-defined micrometer-sized spherical particles under specific physicochemical conditions. These particles are spontaneously built following two main steps: first the formation of oligomers constituting the elementary pieces of the final assembly, second the growth of the particles by assembly of these oligomers (1-3). We hypothezised that the adsorption steps at the air water interface would reflects the assembly mechanism leading to the micro-spheres. To test this hypothesis, we have recorded adsorption kinetics at the air-water interface, of LYS and ALA in conditions where microspheres were formed and in conditions where microspheres could not grow up (i.e. at high ionic strength). Our results show that the adsorption of the mixture LYS-ALA at the air-water interface is governed by the same rules that govern the first steps of formation of micro-spheres.
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Dates et versions

hal-01209658 , version 1 (03-06-2020)

Identifiants

  • HAL Id : hal-01209658 , version 1
  • PRODINRA : 264779

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Stephane Pezennec, Said Bouhallab, Pascaline Hamon, Anne Renault, Sylvie Beaufils. The bulk association mechanism between lysozyme and α-lactalbumine is revealed by interfacial measurements. 14.International Conference on Organized Molecular Films, Jul 2012, Paris, France. , 2012. ⟨hal-01209658⟩
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