Investigation of Bovine Serum Albumin (BSA) Attachment onto Self-Assembled Monolayers (SAMs) Using Combinatorial Quartz Crystal Microbalance with Dissipation (QCM-D) and Spectroscopic Ellipsometry (SE)

Abstract

Understanding protein adsorption kinetics to surfaces is of importance for various environmental and biomedical applications. Adsorption of bovine serum albumin to various self-assembled monolayer surfaces including neutral and charged hydrophilic and hydrophobic surfaces was investigated using in-situ combinatorial quartz crystal microbalance with dissipation and spectroscopic ellipsometry. Adsorption of bovine serum albumin varied as a function of surface properties, bovine serum albumin concentration and pH value. Charged surfaces exhibited a greater quantity of bovine serum albumin adsorption, a larger bovine serum albumin layer thickness, and increased density of bovine serum albumin protein compared to neutral surfaces at neutral pH value. The quantity of adsorbed bovine serum albumin protein increased with increasing bovine serum albumin concentration. After equilibrium sorption was reached at pH 7.0, desorption of bovine serum albumin occurred when pH was lowered to 2.0, which is below the isoelectric point of bovine serum albumin. Our data provide further evidence that combinatorial quartz crystal microbalance with dissipation and spectroscopic ellipsometry is a sensitive analytical tool to evaluate attachment and detachment of adsorbed proteins in systems with environmental implications.

Reactive Maleimido Dextran Thin Films for Cysteine-Containing Surfaces Adsorbing BSA

“…The dimensions of a single BSA molecule are 4 nm × 4 nm × 14 nm in aqueous solution . Thus, the BSA monolayer seems to be a mixture of the side‐on as well as the end‐on scenario . Considering the adsorption kinetic in detail, an overshoot effect takes place for adsorption of BSA on the surface (Figure , top).…”

“…Usually, bovine serum albumin (BSA) is adsorbed as a monolayer on a polymeric substrate that changes the surface properties to prevent other biological molecules from adsorbing . BSA is a globular protein with a size of around 4 nm × 4 nm × 14 nm in aqueous solution and can adsorb to a substrate side‐on or end‐on depending on the surface properties. It is up to materials chemistry to design convenient surfaces adsorbing a dense BSA layer.…”

Complex Polysaccharide-Based Nanocomposites for Oral Insulin Delivery

“…Therefore, no attractive electrostatic interaction among polyelectrolytes takes part, and hydrogen bonding among chains becomes the main force, determining the gelation of the alginate [44,45], as well as the interaction among PEG and poloxamer with polyelectrolytes. Nevertheless, given that under high ionic strength conditions no aggregation was observed, despite the screening of charges, it is more likely that the denaturation of the BSA, which occurred at pH 2, is the triggering process [46].…”

Biosensing Using a Simple Resistor: The Effect of Functionalization on Sensing Devices

“…The abundance of BSA is marked by the wealth of studies that involve it despite already been extensively researched before. Phan et al [11] studied BSA attachment on self-assembled monomers and discovered that charged surfaces allow for great BSA adsorption. They also noted that adsorption happens below pH = 2 which is lower than the isoelectric point of BSA.…”