Calorimetric study of bovine serum albumin dilution and adsorption onto polystyrene particles.

Abstract:

: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).

journal_name

Int J Pharm

authors

Pollitt MJ,Buckton G,Brocchini S,Alpar HO

doi

10.1016/j.ijpharm.2005.02.037

keywords:

subject

Has Abstract

pub_date

2005-07-25 00:00:00

pages

333-8

issue

2

eissn

0378-5173

issn

1873-3476

pii

S0378-5173(05)00240-1

journal_volume

298

pub_type

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