Charge and size drive spontaneous self-assembly of oppositely charged globular proteins into microspheres.

Abstract : 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 the ability of oppositely charged globular proteins to self-assemble into well-defined micrometer-sized spherical particles under specific physicochemical conditions. We show that microspheres were spontaneously formed in all binary protein mixtures tested once the physicochemical conditions were optimized. The optimal pH value, initial protein concentrations needed to form microspheres, and protein stoichiometry in these microspheres varied and depended on the structural features of the mixed proteins. We show that charge compensation is required but not sufficient to guide optimal protein assembly and organization into microspheres. Size difference between protein couples (acidic and basic) is a key element that defines optimal pH value for microsphere formation and the protein molar ratio in the formed microspheres. Our findings give new elements that can help to predict the assembly behavior of various proteins in mixed systems.
Type de document :
Article dans une revue
Journal of Physical Chemistry B, American Chemical Society, 2010, 114 (12), pp.4138-44. 〈10.1021/jp9090427〉
Liste complète des métadonnées

https://hal-agrocampus-ouest.archives-ouvertes.fr/hal-00729460
Contributeur : Céline Martel <>
Soumis le : vendredi 7 septembre 2012 - 15:41:36
Dernière modification le : mercredi 21 mars 2018 - 16:08:07

Identifiants

Citation

Y. Desfougeres, Thomas Croguennec, Valérie Lechevalier-Datin, S. Bouhallab, Françoise Nau. Charge and size drive spontaneous self-assembly of oppositely charged globular proteins into microspheres.. Journal of Physical Chemistry B, American Chemical Society, 2010, 114 (12), pp.4138-44. 〈10.1021/jp9090427〉. 〈hal-00729460〉

Partager

Métriques

Consultations de la notice

80