Cargando…

Electrode Potential-Dependent Studies of Protein Adsorption on Ti(6)Al(4)V Alloy

This article presents the potential-dependent adsorption of two proteins, bovine serum albumin (BSA) and lysozyme (LYZ), on Ti(6)Al(4)V alloy at pH 7.4 and 37 °C. The adsorption process was studied on an electropolished alloy under cathodic and anodic overpotentials, compared to the open circuit pot...

Descripción completa

Detalles Bibliográficos
Autores principales: Duderija, Belma, González-Orive, Alejandro, Ebbert, Christoph, Neßlinger, Vanessa, Keller, Adrian, Grundmeier, Guido
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10343353/
https://www.ncbi.nlm.nih.gov/pubmed/37446771
http://dx.doi.org/10.3390/molecules28135109
_version_ 1785072716855902208
author Duderija, Belma
González-Orive, Alejandro
Ebbert, Christoph
Neßlinger, Vanessa
Keller, Adrian
Grundmeier, Guido
author_facet Duderija, Belma
González-Orive, Alejandro
Ebbert, Christoph
Neßlinger, Vanessa
Keller, Adrian
Grundmeier, Guido
author_sort Duderija, Belma
collection PubMed
description This article presents the potential-dependent adsorption of two proteins, bovine serum albumin (BSA) and lysozyme (LYZ), on Ti(6)Al(4)V alloy at pH 7.4 and 37 °C. The adsorption process was studied on an electropolished alloy under cathodic and anodic overpotentials, compared to the open circuit potential (OCP). To analyze the adsorption process, various complementary interface analytical techniques were employed, including PM-IRRAS (polarization-modulation infrared reflection-absorption spectroscopy), AFM (atomic force microscopy), XPS (X-ray photoelectron spectroscopy), and E-QCM (electrochemical quartz crystal microbalance) measurements. The polarization experiments were conducted within a potential range where charging of the electric double layer dominates, and Faradaic currents can be disregarded. The findings highlight the significant influence of the interfacial charge distribution on the adsorption of BSA and LYZ onto the alloy surface. Furthermore, electrochemical analysis of the protein layers formed under applied overpotentials demonstrated improved corrosion protection properties. These studies provide valuable insights into protein adsorption on titanium alloys under physiological conditions, characterized by varying potentials of the passive alloy.
format Online
Article
Text
id pubmed-10343353
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-103433532023-07-14 Electrode Potential-Dependent Studies of Protein Adsorption on Ti(6)Al(4)V Alloy Duderija, Belma González-Orive, Alejandro Ebbert, Christoph Neßlinger, Vanessa Keller, Adrian Grundmeier, Guido Molecules Article This article presents the potential-dependent adsorption of two proteins, bovine serum albumin (BSA) and lysozyme (LYZ), on Ti(6)Al(4)V alloy at pH 7.4 and 37 °C. The adsorption process was studied on an electropolished alloy under cathodic and anodic overpotentials, compared to the open circuit potential (OCP). To analyze the adsorption process, various complementary interface analytical techniques were employed, including PM-IRRAS (polarization-modulation infrared reflection-absorption spectroscopy), AFM (atomic force microscopy), XPS (X-ray photoelectron spectroscopy), and E-QCM (electrochemical quartz crystal microbalance) measurements. The polarization experiments were conducted within a potential range where charging of the electric double layer dominates, and Faradaic currents can be disregarded. The findings highlight the significant influence of the interfacial charge distribution on the adsorption of BSA and LYZ onto the alloy surface. Furthermore, electrochemical analysis of the protein layers formed under applied overpotentials demonstrated improved corrosion protection properties. These studies provide valuable insights into protein adsorption on titanium alloys under physiological conditions, characterized by varying potentials of the passive alloy. MDPI 2023-06-29 /pmc/articles/PMC10343353/ /pubmed/37446771 http://dx.doi.org/10.3390/molecules28135109 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Duderija, Belma
González-Orive, Alejandro
Ebbert, Christoph
Neßlinger, Vanessa
Keller, Adrian
Grundmeier, Guido
Electrode Potential-Dependent Studies of Protein Adsorption on Ti(6)Al(4)V Alloy
title Electrode Potential-Dependent Studies of Protein Adsorption on Ti(6)Al(4)V Alloy
title_full Electrode Potential-Dependent Studies of Protein Adsorption on Ti(6)Al(4)V Alloy
title_fullStr Electrode Potential-Dependent Studies of Protein Adsorption on Ti(6)Al(4)V Alloy
title_full_unstemmed Electrode Potential-Dependent Studies of Protein Adsorption on Ti(6)Al(4)V Alloy
title_short Electrode Potential-Dependent Studies of Protein Adsorption on Ti(6)Al(4)V Alloy
title_sort electrode potential-dependent studies of protein adsorption on ti(6)al(4)v alloy
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10343353/
https://www.ncbi.nlm.nih.gov/pubmed/37446771
http://dx.doi.org/10.3390/molecules28135109
work_keys_str_mv AT duderijabelma electrodepotentialdependentstudiesofproteinadsorptiononti6al4valloy
AT gonzalezorivealejandro electrodepotentialdependentstudiesofproteinadsorptiononti6al4valloy
AT ebbertchristoph electrodepotentialdependentstudiesofproteinadsorptiononti6al4valloy
AT neßlingervanessa electrodepotentialdependentstudiesofproteinadsorptiononti6al4valloy
AT kelleradrian electrodepotentialdependentstudiesofproteinadsorptiononti6al4valloy
AT grundmeierguido electrodepotentialdependentstudiesofproteinadsorptiononti6al4valloy