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)

Authors

Hanh T.M. Phan, University of Nebraska-LincolnFollow
Shannon L. Bartelt-Hunt, University of Nebraska-LincolnFollow
Keith B. Rodenhausen, University of Nebraska-LincolnFollow
Mathias Schubert, University of Nebraska - LincolnFollow
Jason C. Bartz, Creighton UniversityFollow

Document Type

Article

Date of this Version

9-2015

Citation

Phan HTM, Bartelt-Hunt S, Rodenhausen KB, Schubert M, Bartz JC (2015) Investigation of Bovine Serum Albumin (BSA) Attachment onto Self- Assembled Monolayers (SAMs) Using Combinatorial Quartz Crystal Microbalance with Dissipation (QCMD) and Spectroscopic Ellipsometry (SE). PLoS ONE 10(10): e0141282. doi:10.1371/journal.pone.0141282
October 27, 2015

Comments

© 2015 Phan et al. This is an open access article distributed under the terms of the Creative Commons Attribution License

Abstract

Understanding protein adsorption kinetics to surfaces is of importance for various environmental and biomedical applications. Adsorption of bovine serum albumin to various selfassembled 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.