title: 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.
authors.affiliation: UMR 1253, INRA, Agrocampus-Ouest, STLO, Rennes, France.
authors.forename: Delphine
authors.initials: D
authors.lastname: Salvatore
authors.forename: Thomas
authors.initials: T
authors.lastname: Croguennec
authors.forename: Saïd
authors.initials: S
authors.lastname: Bouhallab
authors.forename: Vincent
authors.initials: V
authors.lastname: Forge
authors.forename: Taco
authors.initials: T
authors.lastname: Nicolai
mesh_terms: D007700:Kinetics; D018613:Microscopy, Confocal; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012996:Solutions; D014867:Water
chemical_list: D011506:Proteins; D012996:Solutions; D014867:Water