Scaling the Structure Factors of Protein Limit Colloid−Polymer Mixtures

• Published in: Langmuir Vol. 26; no. 3; pp. 1630 - 1634
• Main Authors: Mutch, Kevin J, van Duijneveldt, Jeroen S, Eastoe, Julian, Grillo, Isabelle, Heenan, Richard K
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 02.02.2010
• Subjects: Chemistry; Colloidal state and disperse state; Colloids; Colloids: Surfactants and Self-Assembly, Dispersions, Emulsions, Foams; Emulsions. Microemulsions. Foams; Exact sciences and technology; General and physical chemistry; Phase Transition; Polymers - chemistry; Proteins - chemistry; Surface physical chemistry; Thermodynamics; Structure factor; Thermodynamics; Stability; Polymer; Droplet; Microemulsion; Colloid; Protein
• ISSN: 0743-7463; 1520-5827
• DOI: 10.1021/la902508z

The scaling of the phase boundaries and structure factors of protein limit colloid−polymer mixtures has been investigated through the addition of large nonadsorbing polymer chains to a solution of small microemulsion droplets. The colloid−polymer size ratio has been varied between 10 and 16 by changing the microemulsion droplet size; the phase boundaries were shown previously to observe theoretical scaling relations very well [Langmuir 2009, 25 (7), 3944−3952]. These thermodynamic scaling relations are now shown to also hold extremely well for the individual and cross-term partial structure factors. The structure factors for systems with different size ratios occupying the same point in scaled phase space show extremely good agreement. The properties and stability of these mixtures are governed by the polymer mesh.