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Photo-renaturation de protéines par des macromolécules chaperonnes

Abstract : We wanted to design macromolecules that behave like artificial chaperones with different proteins and form which the motor will be light-stimulation. Hydrophobic interactions are proved to be a key point of the chaperone effect both in biological and artificial chaperones. We synthesized polymers with azobenzene moities that have a light-triggered amphiphily. These polymers were shown to be able to photo-associate and photo-dissociate with colloidal partners like micelles or proteins. The parameters that can modulate these associations are ionic strength, hydrophobic modification rate, nature of azobenzene moities... These polymers have exhibited some features of artificial chaperones: they destabilize a model protein like cythochrome~C, they prevent from aggregation and improve the efficiency of the renaturation process of carbonic anhydrase and of an antibody fragment overexpressed in bacteria. The refolding was monitored by following the evolution of secondary structures by circular dichroism and the evolution of the compacity of the protein by fluorescence. The polymer/protein association was studied by capillary electrophoresis and light scattering.
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Contributor : Juliette Ruchmann <>
Submitted on : Wednesday, March 17, 2010 - 5:10:59 PM
Last modification on : Wednesday, October 14, 2020 - 3:43:20 AM
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  • HAL Id : tel-00464683, version 1

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Juliette Ruchmann. Photo-renaturation de protéines par des macromolécules chaperonnes. Matériaux. ESPCI ParisTECH, 2009. Français. ⟨tel-00464683⟩

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