Influence of surface charge on the rate, extent, and structure of adsorbed Bovine Serum Albumin to gold electrodes

Burcu Beykal, Moshe Herzberg, Yoram Oren, Meagan S. Mauter

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

The objective of this work is to investigate the rate, extent, and structure of amphoteric proteins with charged solid surfaces over a range of applied potentials and surface charges. We use Electrochemical Quartz Crystal Microbalance with Dissipation Monitoring (E-QCM-D) to investigate the adsorption of amphoteric Bovine Serum Albumin (BSA) to a gold electrode while systematically varying the surface charge on the adsorbate and adsorbent by manipulating pH and applied potential, respectively. We also perform cyclic voltammetry-E-QCM-D on an adsorbed layer of BSA to elucidate conformational changes in response to varied applied potentials. We confirm previous results demonstrating that increasing magnitude of applied potential on the gold electrode is positively correlated with increasing mass adsorption when the protein and the surface are oppositely charged. On the other hand, we find that the rate of BSA adsorption is not governed by simple electrostatics, but instead depends on solution pH, an observation not well documented in the literature. Cyclic voltammetry with simultaneous E-QCM-D measurements suggest that BSA protein undergoes a conformational change as the surface potential varies.

Original languageEnglish
Pages (from-to)321-328
Number of pages8
JournalJournal of Colloid and Interface Science
Volume460
DOIs
StatePublished - 15 Dec 2015

Keywords

  • Bovine serum albumin
  • Cyclic voltammetry
  • Electrochemical QCM-D
  • Protein adsorption

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