| Literature DB >> 15518493 |
Kurosch Rezwan1, Lorenz P Meier, Mandana Rezwan, Janos Vörös, Marcus Textor, Ludwig J Gauckler.
Abstract
We investigated the adsorption of bovine serum albumin (BSA) on colloidal Al2O3 particles in an aqueous environment. Changes in the zeta potential of the Al2O3 particles upon the adsorption of BSA were measured using an electro-acoustic technique. The mass of protein adsorbed was determined by using UV-vis spectroscopy. The change of the isoelectric point of the Al2O3 powder-protein suspension was found to be a function of adsorbed protein mass. It was shown that approximately one monolayer of BSA was needed to fully mask the surface and to compromise the charge of Al2O3. From titration experiments it follows that about 30-36% of the negatively charged groups of the protein form bonds with the protonated and charged Al2O3 surface. On the basis of our observations we introduced a new adsorption model for BSA on Al2O3 particles.Entities:
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Year: 2004 PMID: 15518493 DOI: 10.1021/la048459k
Source DB: PubMed Journal: Langmuir ISSN: 0743-7463 Impact factor: 3.882