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Tetraphenylporphyrin as a protein label for triple detection analytical systems
Porphyrins and metalloporphyrins are promising new protein labels that can be detected using multiple techniques; improving the reliability of the analysis and broadening the range of the linear response. Here, we investigate the potential of 5,10,15,20-tetraphenyl-21H,23H-porphyrin (Tpp) as a hybri...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4945755/ https://www.ncbi.nlm.nih.gov/pubmed/27441235 http://dx.doi.org/10.1016/j.heliyon.2015.e00053 |
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author | Konopińska, Kamila Pietrzak, Mariusz Mazur, Radosław Malinowska, Elżbieta |
author_facet | Konopińska, Kamila Pietrzak, Mariusz Mazur, Radosław Malinowska, Elżbieta |
author_sort | Konopińska, Kamila |
collection | PubMed |
description | Porphyrins and metalloporphyrins are promising new protein labels that can be detected using multiple techniques; improving the reliability of the analysis and broadening the range of the linear response. Here, we investigate the potential of 5,10,15,20-tetraphenyl-21H,23H-porphyrin (Tpp) as a hybrid protein label. The electrochemical and optical properties of porphyrin conjugated with bovine serum albumin (BSA), chicken egg albumin (CEA) and immunoglobulin G (IgG) were determined and optimal conditions for Tpp-protein conjugation established. Model conjugates of carboxylated Tpp with BSA and short peptides were characterized using differential pulse voltammetry, UV–Vis spectrophotometry and spectrofluorimetry. These results reveal that Tpp is a promising molecule to be used in a triple detection protein labelling system. |
format | Online Article Text |
id | pubmed-4945755 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-49457552016-07-20 Tetraphenylporphyrin as a protein label for triple detection analytical systems Konopińska, Kamila Pietrzak, Mariusz Mazur, Radosław Malinowska, Elżbieta Heliyon Article Porphyrins and metalloporphyrins are promising new protein labels that can be detected using multiple techniques; improving the reliability of the analysis and broadening the range of the linear response. Here, we investigate the potential of 5,10,15,20-tetraphenyl-21H,23H-porphyrin (Tpp) as a hybrid protein label. The electrochemical and optical properties of porphyrin conjugated with bovine serum albumin (BSA), chicken egg albumin (CEA) and immunoglobulin G (IgG) were determined and optimal conditions for Tpp-protein conjugation established. Model conjugates of carboxylated Tpp with BSA and short peptides were characterized using differential pulse voltammetry, UV–Vis spectrophotometry and spectrofluorimetry. These results reveal that Tpp is a promising molecule to be used in a triple detection protein labelling system. Elsevier 2015-12-22 /pmc/articles/PMC4945755/ /pubmed/27441235 http://dx.doi.org/10.1016/j.heliyon.2015.e00053 Text en © 2015 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Konopińska, Kamila Pietrzak, Mariusz Mazur, Radosław Malinowska, Elżbieta Tetraphenylporphyrin as a protein label for triple detection analytical systems |
title | Tetraphenylporphyrin as a protein label for triple detection analytical systems |
title_full | Tetraphenylporphyrin as a protein label for triple detection analytical systems |
title_fullStr | Tetraphenylporphyrin as a protein label for triple detection analytical systems |
title_full_unstemmed | Tetraphenylporphyrin as a protein label for triple detection analytical systems |
title_short | Tetraphenylporphyrin as a protein label for triple detection analytical systems |
title_sort | tetraphenylporphyrin as a protein label for triple detection analytical systems |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4945755/ https://www.ncbi.nlm.nih.gov/pubmed/27441235 http://dx.doi.org/10.1016/j.heliyon.2015.e00053 |
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