BSA structural changes during homomolecular exchange between the adsorbed and the dissolved states

WILLEM NORDE; CARLA EUGENIA GIACOMELLI

JOURNAL OF BIOTECHNOLOGY

Elsevier Science B.V.

Año: 2000 vol. 79 p. 259 - 259

0168-1656

font size="1" face="TimesNRMT"> The secondary structure and the thermostability of bovine serum albumin (BSA), before adsorption and after homomolecular displacement from silica and polystyrene particles, are studied by circular dichroism spectroscopy and differential scanning calorimetry. The structural perturbations induced by the hydrophilic silica surface are reversible, i.e. BSA completely regains the native structure and stability after being exchanged. On the other hand, the adsorption on, and subsequent desorption from, polystyrene particles causes irreversible changes in the stability and (secondary) structure of BSA. The exchanged proteins have a higher denaturation temperature and a lower enthalpy of denaturation than native BSA. The a-helix content is reduced while the