PEGylation of platinum bio-electrodes

Abstract

Controlling protein interactions at the implanted electrode interface is becoming an important strategy for the management of foreign body responses that have proven to be detrimental to the long-term performance of neural prosthesis. In this study, PEGylation was conducted on platinum bio-electrodes to render the surface protein-resistant. The PEGylated electrode was investigated using a quartz crystal microbalance-dissipation, electrochemical impedance spectroscopy and cyclic voltammetiy. AbstractControlling protein interactions at the implanted electrode interface is becoming an important strategy for the management of foreign body responses that have proven to be detrimental to the long-term performance of neural prosthesis. In this study, PEGylation was conducted on platinum bio-electrodes to render the surface protein-resistant. The PEGylated electrode was investigated using a quartz crystal microbalance-dissipation, electrochemical impedance spectroscopy and cyclic voltammetry.

Lubricin Antiadhesive Coatings Exhibit Size‐Selective Transport Properties that Inhibit Biofouling of Electrode Surfaces with Minimal Loss in Electrochemical Activity

“…One possible explanation is that the chains of the PEG brush are packed too densely for the K 3 [Fe(CN) 6 ] redox couple to diffuse freely across this boundary. Other examples of cyclic voltammetry measurements performed with PEG coated electrodes and K 3 [Fe(CN) 6 ] redox couple can be found in the literature and, while these studies do not report a total passivation as seen in Figure f, the passivation effects that are observed are still quite significant even without any fouling molecules present in the testing solution. These other example systems utilized platinum and carbon electrodes.…”

“…Direct modification of electrode surfaces with self‐assembling antiadhesive molecules, typically polyethylene glycol (PEG), is an alternative approach that has been used with limited success. The main drawback of direct modification of electrode surfaces with antifouling agents is that they too often passivate the electrode with detrimental effects on amperometric or voltammetric sensing and are instead more suitable for optical or impedimetric approaches …”

Investigation of the Antifouling Properties of Phenyl Phosphorylcholine‐Based Modified Gold Surfaces

“…Nonspecific protein adsorption on an electrode may lead to a decrease in sensor selectivity by interfering with the interaction of target species with the sensing surface, or may result in fluctuations in sensor sensitivity by blocking the electron transfer pathway of redox active species 1. Furthermore, for implantable electrodes, the initiation of protein adsorption often provokes the immune and coagulation systems 6–7. Hence the antifouling capability of an electrode is crucial for electrodes used in biological fluids 4, 5, 8.…”

Impact of Protein Fouling on the Charge Injection Capacity, Impedance, and Effective Electrode Area of Platinum Electrodes for Bionic Devices

“…Previous atomic force microscopy and ellipsometry measurements of platinum in contact with protein containing solutions displayed an increase in adsorbed layer thickness and roughness over time [30] . And quartz crystal microbalance studies of platinum placed in contact with protein containing solutions have shown a mass increase on the electrode, consistent with protein adsorption [31] . It was found that exposure of platinum to protein containing solutions for 10 minutes induced reproducible, steady‐state mass adsorption.…”

“…[30] And quartz crystal microbalance studies of platinum placed in contact with protein containing solutions have shown a mass increase on the electrode, consistent with protein adsorption. [31] It was found that exposure of platinum to protein containing solutions for 10 minutes induced reproducible, steady-state mass adsorption. BSA, fibrinogen and trypsin inhibitor were chosen as low cost, readily available proteins that represent 3 of the highest concentration protein classes (albumins, glycoproteins, and protease inhibitors) in perilymph.…”