A neutron reflection study of adsorbed deuterated myoglobin layers on hydrophobic surfaces

Protein Adsorption, Desorption, and Aggregation Mediated by Solid-Liquid Interfaces

“…However, the primary focus of most research has been on changes in protein conformation and/or ligand binding for proteins that remain physically or chemically bound to the surface, rather than assessing subsequent aggregate formation and the presence of detectable aggregates in bulk solution. Previous work suggests that adsorption of proteins to hydrophilic surfaces is primarily dictated by electrostatic surface–protein interactions, whereas the prevalence of nonpolar patches on the surface of a protein is more important in determining adsorption to hydrophobic surfaces …”

“…SiOx, a primary component of glass vials used for biopharmaceutical products and/or manufacturing, was chosen to mimic the walls of vials. By using this material, it is also relatively straightforward to obtain sufficiently smooth and flat surfaces that permit high‐resolution NR measurements for adsorption of proteins or similarly sized nanoparticles . The packing density and surface thickness of adsorbed proteins was determined as a function of solution pH and ionic strength, as well as changes in the surface layer(s) upon gentle rinsing with buffer solution.…”

“…Previous work suggests that adsorption of proteins to hydrophilic surfaces is primarily dictated by electrostatic surface-protein interactions, whereas the prevalence of nonpolar patches on the surface of a protein is more important in determining adsorption to hydrophobic surfaces. [15][16][17][18][19][20][21][22] The present work focuses on aggregation mediated by adsorption to aqueous interfaces with silicon oxide (SiOx) for two model proteins: a relatively small (ß26 kDa) globular protein, alpha-chymotrypsinogen (aCgn); and a larger (ß150 kDa), multidomain immunoglobulin gamma-1 (IgG1) ( Fig. 1).…”

“…By using this material, it is also relatively straightforward to obtain sufficiently smooth and flat surfaces that permit high-resolution NR measurements for adsorption of proteins or similarly sized nanoparticles. 5,16,21,[23][24][25][26] The packing density and surface thickness of adsorbed proteins was determined as a function of solution pH and ionic strength, as well as changes in the surface layer(s) upon gentle rinsing with buffer solution. Desorption of the proteins from SiOx was initiated by a series of buffer rinses and followed by observing the conformational changes in the adsorbed layer, as well as the presence of aggregates in the rinse solution.…”

Mechanism of Myoglobin Molecule Adsorption on Silica: QCM, OWLS and AFM Investigations

“…The influence of myoglobin concentration on the structure of its layers at different hydrophobic surfaces (polystyrene and octadecyltrichlorosilane) was studied in ref. [ 30 ] by neutron reflectometry. Because the protein layers exhibited hydrophilic properties, it was postulated that myoglobin molecules are attached to the substrates by their hydrophobic parts and expose the hydrophilic parts into the bulk solution.…”