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, i.e. 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.

arXiv comment17 pages, 5 figures

References in corpus (1)

• Capillary Condensation, Freezing, and Melting in Silica Nanopores: A Sorption Isotherm and Scanning Calorimetry Study on Nitrogen in Mesoporous SBA-15

Cited by in corpus (3)

• Soft matter in hard confinement: phase transition thermodynamics, structure, texture, diffusion and flow in nanoporous media - topical review
• pH-Dependent Selective Protein Adsorption into Mesoporous Silica
• Critical adsorption of polyelectrolytes onto planar and convex highly charged surfaces: the nonlinear Poisson-Boltzmann approach