Modification of gold surfaces for the oriented immobilization of recombinant form of horseradish peroxidase
Gold threads of 0.50mmof diameter and 25mmin length were used as work electrodes. These electrodes were electrochemically characterized and their effective areas were determined. The gold surface was chemically modified with a self-assembled monolayer of thiols (SAMs) and, by means of successive re...
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Format: | Article |
Language: | English |
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Universidad del Zulia
2010-05-01
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Series: | Revista Técnica de la Facultad de Ingeniería |
Online Access: | https://www.produccioncientificaluz.org/index.php/tecnica/article/view/6195 |
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author | Pedro Rafael Matheus José María Abad Víctor Manuel Fernández |
author_facet | Pedro Rafael Matheus José María Abad Víctor Manuel Fernández |
author_sort | Pedro Rafael Matheus |
collection | DOAJ |
description | Gold threads of 0.50mmof diameter and 25mmin length were used as work electrodes. These electrodes were electrochemically characterized and their effective areas were determined. The gold surface was chemically modified with a self-assembled monolayer of thiols (SAMs) and, by means of successive reactions, they get bonded covalently to the thiols monolayer, ligands with chelates metallic ion groups (derived from the nitrilotriacetic acid, ANTA) which show affinity by surface receptors generated in a genetic enzyme via engineering techniques. The obtained results showed the good sensitivity, specificity and stability of the used electrochemical techniques in this work.
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first_indexed | 2024-04-11T06:23:18Z |
format | Article |
id | doaj.art-b9335c882be54fb19b57993788ca9224 |
institution | Directory Open Access Journal |
issn | 0254-0770 2477-9377 |
language | English |
last_indexed | 2024-04-11T06:23:18Z |
publishDate | 2010-05-01 |
publisher | Universidad del Zulia |
record_format | Article |
series | Revista Técnica de la Facultad de Ingeniería |
spelling | doaj.art-b9335c882be54fb19b57993788ca92242022-12-22T04:40:31ZengUniversidad del ZuliaRevista Técnica de la Facultad de Ingeniería0254-07702477-93772010-05-01303Modification of gold surfaces for the oriented immobilization of recombinant form of horseradish peroxidasePedro Rafael Matheus0José María Abad1Víctor Manuel Fernández2Universidad de Los Andes-VenezuelaInstituto de Catálisis y Petroleoquímica-EspañaUniversidad de Los Andes-Venezuela Gold threads of 0.50mmof diameter and 25mmin length were used as work electrodes. These electrodes were electrochemically characterized and their effective areas were determined. The gold surface was chemically modified with a self-assembled monolayer of thiols (SAMs) and, by means of successive reactions, they get bonded covalently to the thiols monolayer, ligands with chelates metallic ion groups (derived from the nitrilotriacetic acid, ANTA) which show affinity by surface receptors generated in a genetic enzyme via engineering techniques. The obtained results showed the good sensitivity, specificity and stability of the used electrochemical techniques in this work. https://www.produccioncientificaluz.org/index.php/tecnica/article/view/6195 |
spellingShingle | Pedro Rafael Matheus José María Abad Víctor Manuel Fernández Modification of gold surfaces for the oriented immobilization of recombinant form of horseradish peroxidase Revista Técnica de la Facultad de Ingeniería |
title | Modification of gold surfaces for the oriented immobilization of recombinant form of horseradish peroxidase |
title_full | Modification of gold surfaces for the oriented immobilization of recombinant form of horseradish peroxidase |
title_fullStr | Modification of gold surfaces for the oriented immobilization of recombinant form of horseradish peroxidase |
title_full_unstemmed | Modification of gold surfaces for the oriented immobilization of recombinant form of horseradish peroxidase |
title_short | Modification of gold surfaces for the oriented immobilization of recombinant form of horseradish peroxidase |
title_sort | modification of gold surfaces for the oriented immobilization of recombinant form of horseradish peroxidase |
url | https://www.produccioncientificaluz.org/index.php/tecnica/article/view/6195 |
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