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Updated: May 2, 2026

Monitoring Protein Adsorption with Solid-state Nanopores
Published on: December 2, 2011
Protein adsorption into mesopores: a combination of electrostatic interaction, counterion release, and van der Waals
Sebastian T Moerz1, Patrick Huber
1Experimental Physics, Saarland University , D-66041 Saarbrücken, Germany.
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.
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