Adsorption of Lysozyme Into a Charged Confining Pore

Several applications arise from the confinement of proteins on surfaces since their stability and biological activity are enhanced. It is also known that the way a protein adsorbs on the surface is important for its biological function since its active sites should not be obstructed. In this study, the adsorption properties of hen egg-white Lysozyme, HEWL, into a negatively charged silica pore is examined employing a coarse-grained model and constant-pH Monte Carlo simulations. The role of electrostatic interactions is taken into account when including the Debye-Hueckel potentials into the Ca structure-based model. We evaluate the effects of pH, salt concentration, and pore radius on the protein preferential orientation and spatial distribution of its residues regarding the pore surface. By mapping the residues that stay closer to the pore surface, we find the increase of pH leads to orientational changes of the adsorbed protein when the solution pH gets closer to the HEWL isoelectric point. At these conditions, the pKa shift of these important residues caused by the adsorption into the charged confining surface results in a HEWL charge distribution that stabilizes the adsorption in the observed protein orientation. We compare our observations to the results of pKa shift for HEWL available in the literature and to some experimental data.

Highly efficient complexation of sanguinarine alkaloid by carboxylatopillar[6]arene: pKa shift, increased solubility and enhanced antibacterial activity

Efficient complexation of sanguinarine by carboxylatopillar[6]arene. The pKa shift, increased solubility, and enhanced antibacterial activity are described.

Fluorescence enhancement and pKa shift of a rho kinase inhibitor by a synthetic receptor

The significant fluorescence enhancement and pKa shift of fasudil upon encapsulation by cucurbit[7]uril may provide a traceable enteric formulation.