Kinetics and structure during self-assembly of oppositely charged proteins in aqueous solution.

Abstract : Self-assembly in aqueous solution of two oppositely charged globular proteins, hen egg white lysozyme (LYS) and bovine calcium-depleted α-lactalbumin (apo α-LA), was investigated at pH 7.5. The aggregation rate of equimolar mixtures of the two proteins was determined using static and dynamic light scattering as a function of the ionic strength (15-70 mM) and protein concentration (0.28-2.8 g/L) at 25 and 45 °C. The morphology of formed supramolecular structures was observed by confocal laser scanning microscopy. When the two proteins are mixed, small aggregates were formed rapidly that subsequently grew by collision and fusion. The aggregation process led on larger length scales to irregularly shaped flocs at 25 °C, but to monodisperse homogeneous spheres at 45 °C. Both the initial rate of aggregation and the fraction of proteins that associated decreased strongly with decreasing protein concentration or increasing ionic strength but was independent of the temperature.
Type de document :
Article dans une revue
Biomacromolecules, American Chemical Society, 2011, 12 (5), pp.1920-6. 〈10.1021/bm200264m〉
Liste complète des métadonnées

https://hal-agrocampus-ouest.archives-ouvertes.fr/hal-00729258
Contributeur : Céline Martel <>
Soumis le : vendredi 7 septembre 2012 - 15:30:54
Dernière modification le : mercredi 21 mars 2018 - 16:08:07

Identifiants

Citation

D.B. Salvatore, Thomas Croguennec, S. Bouhallab, V. Forge, T. Nicolai. Kinetics and structure during self-assembly of oppositely charged proteins in aqueous solution.. Biomacromolecules, American Chemical Society, 2011, 12 (5), pp.1920-6. 〈10.1021/bm200264m〉. 〈hal-00729258〉

Partager

Métriques

Consultations de la notice

121