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)

Hanh T M Phan; Shannon Bartelt-Hunt; Keith B Rodenhausen; Mathias Schubert; Jason C Bartz

doi:10.1371/journal.pone.0141282

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)

PLoS One. 2015 Oct 27;10(10):e0141282. doi: 10.1371/journal.pone.0141282. eCollection 2015.

Authors

Hanh T M Phan¹, Shannon Bartelt-Hunt¹, Keith B Rodenhausen², Mathias Schubert², Jason C Bartz³

Affiliations

¹ Department of Civil Engineering, University of Nebraska-Lincoln, Lincoln, Nebraska, United States of America.
² Department of Electrical and Computer Engineering, University of Nebraska-Lincoln, Lincoln, Nebraska, United States of America.
³ Department of Medical Microbiology and Immunology, Creighton University, Omaha, Nebraska, United States of America.

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.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Adsorption
Animals
Cattle
Coated Materials, Biocompatible / chemistry*
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Nuclear Magnetic Resonance, Biomolecular
Quartz Crystal Microbalance Techniques*
Serum Albumin, Bovine / chemistry*
Surface Properties

Substances

Coated Materials, Biocompatible
Serum Albumin, Bovine

Grants and funding

Funding for this work was provided by the National Science Foundation (www.nsf.gov) (award CBET-1149242 to SB and award EPS-1004094 to MS). The funders had no role in study design, data collection and analysis, decision to publish or preparation of the manuscript.