Interaction between lysozyme and colloidal poly(NIPAM-co-acrylic acid) microgels.
The interaction between lysozyme and colloidal poly(NIPAM-co-acrylic acid) microgels is investigated in aqueous solutions at neutral pH. Lysozyme binding isotherms, obtained within the ionic strength range 10-220 mM, indicate that the maximum uptake at 10 mM is 2.4 g lysozyme per gram dry gel, and that the uptake capacity decreases with increasing ionic strength to approximately 0 at 220 mM. Swelling isotherms, obtained from photon correlation spectroscopy measurements, show that the binding is accompanied by a substantial deswelling of the microgels. The microgel suspension is stable up to a protein-to-polymer charge ratio in the microgels of about 0.6, largely independent of ionic strength, whereas flocculation/sedimentation occurs at higher charge ratios. The charge ratio 0.6 corresponds to a zeta-potential of about -6 mV, as obtained from measurements of electrophoretic mobility. Binding and swelling isotherms are analyzed in detail and compared with predictions of theoretical model calculations. The influence of protein-protein attraction is highlighted, as well as the interplay between electrostatic interactions and network elasticity.
Johansson
Christian
C
Department of Pharmacy, Uppsala University, Box 580, SE-75123 Uppsala, Sweden.
Gernandt
Jonas
J
Bradley
Melanie
M
Vincent
Brian
B
Hansson
Per
P
D000179:Acrylates; D000180:Acrylic Resins / Q000737:chemistry*; D003102:Colloids / Q000737:chemistry; D004548:Elasticity; D005782:Gels / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D055672:Static Electricity
D000179:Acrylates; D000180:Acrylic Resins; D003102:Colloids; D005782:Gels; C052970:poly-N-isopropylacrylamide; D009113:Muramidase; C036658:acrylic acid