title: Protein adsorption into mesopores: a combination of electrostatic interaction, counterion release, and van der Waals forces.
abstract: Bovine heart cytochrome c has been immobilized into the mesoporous silica host material SBA-15 in both its native folded and urea-unfolded state. The comparison of the two folding states' behavior casts doubt on the commonly used explanation of cytochrome c adsorption, that is, the electrostatic interaction model. A detailed investigation of the protein binding as a function of pH and ionic strength of the buffer solution reveals the complex nature of the protein-silica interaction. Electrostatic interaction, van der Waals forces, and entropic contributions by counterion release each contribute to adsorption on the silica pore walls.
authors.affiliation: Experimental Physics, Saarland University , D-66041 Saarbrücken, Germany.
authors.forename: Sebastian T
authors.initials: ST
authors.lastname: Moerz
authors.forename: Patrick
authors.initials: P
authors.lastname: Huber
mesh_terms: D000327:Adsorption; D000818:Animals; D002417:Cattle; D045304:Cytochromes c; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D012822:Silicon Dioxide / Q000737:chemistry*; D055672:Static Electricity; D013816:Thermodynamics
chemical_list: D011506:Proteins; C509969:SBA-15; D012822:Silicon Dioxide; D045304:Cytochromes c