Calorimetric study of bovine serum albumin dilution and adsorption onto polystyrene particles.
Titration calorimetry was used to investigate the interaction between a model antigen, bovine serum albumin (BSA), and a model particulate carrier, polystyrene (PS). The binding enthalpy was much higher than reported in the literature for a similar system and did not display a sigmoidal binding curve. These experiments may have accessed low coverage surface sites due to the irreversible nature of protein binding and stepwise titration. An important correction is the heat of dilution of the protein solution. Two regimes were observed: at low concentrations of BSA (below ca. 0.3% (w/v)) an exothermic dilution enthalpy of ca. -100 mJ mg-1 was determined, whereas at higher concentrations of BSA values of ca. -20 mJ mg-1 were obtained. Solution rheological data also showed a change at 0.3% (w/v) BSA, so we hypothesise that the fraction of the BSA as monomers, dimers and polymers in solution changes at approximately 0.3% (w/v).
Pollitt
M J
MJ
Department of Pharmaceutics, School of Pharmacy, 29-39 Brunswick Square, London WC1N 1AX, UK. michael.pollitt@ulsop.ac.uk
Buckton
G
G
Brocchini
S
S
Alpar
H O
HO
D000327:Adsorption; D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D049329:Nanostructures; D010316:Particle Size; D011137:Polystyrenes; D012212:Rheology; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013816:Thermodynamics
D011137:Polystyrenes; D012710:Serum Albumin, Bovine