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Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide
The main objective of the presented study was the development of a simple analytical tool for exploring the influence of naturally occurring compounds on the aggregation of amyloid-β peptide (Aβ(40)) in order to find potential anti-neurodegenerative drugs. The gold discs used for surface plasmon res...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3231330/ https://www.ncbi.nlm.nih.gov/pubmed/22163834 http://dx.doi.org/10.3390/s110404030 |
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author | Kraziński, Bartłomiej Emil Radecki, Jerzy Radecka, Hanna |
author_facet | Kraziński, Bartłomiej Emil Radecki, Jerzy Radecka, Hanna |
author_sort | Kraziński, Bartłomiej Emil |
collection | PubMed |
description | The main objective of the presented study was the development of a simple analytical tool for exploring the influence of naturally occurring compounds on the aggregation of amyloid-β peptide (Aβ(40)) in order to find potential anti-neurodegenerative drugs. The gold discs used for surface plasmon resonance (SPR) measurements were modified with thioaliphatic acid. The surface functionalized with carboxylic groups was used for covalent attaching of Aβ(40) probe by creation of amide bonds in the presence of EDC/NHS. The modified SPR gold discs were used for exploring the Aβ(40) aggregation process in the presence of selected alkaloids: arecoline hydrobromide, pseudopelletierine hydrochloride, trigonelline hydrochloride and α-lobeline hydrochloride. The obtained results were discussed with other parameters which govern the phenomenon studied such as lipophilicity/hydrophilicy and Aβ(40)-alkaloid association constants. |
format | Online Article Text |
id | pubmed-3231330 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-32313302011-12-07 Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide Kraziński, Bartłomiej Emil Radecki, Jerzy Radecka, Hanna Sensors (Basel) Article The main objective of the presented study was the development of a simple analytical tool for exploring the influence of naturally occurring compounds on the aggregation of amyloid-β peptide (Aβ(40)) in order to find potential anti-neurodegenerative drugs. The gold discs used for surface plasmon resonance (SPR) measurements were modified with thioaliphatic acid. The surface functionalized with carboxylic groups was used for covalent attaching of Aβ(40) probe by creation of amide bonds in the presence of EDC/NHS. The modified SPR gold discs were used for exploring the Aβ(40) aggregation process in the presence of selected alkaloids: arecoline hydrobromide, pseudopelletierine hydrochloride, trigonelline hydrochloride and α-lobeline hydrochloride. The obtained results were discussed with other parameters which govern the phenomenon studied such as lipophilicity/hydrophilicy and Aβ(40)-alkaloid association constants. Molecular Diversity Preservation International (MDPI) 2011-04-06 /pmc/articles/PMC3231330/ /pubmed/22163834 http://dx.doi.org/10.3390/s110404030 Text en © 2011 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Kraziński, Bartłomiej Emil Radecki, Jerzy Radecka, Hanna Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide |
title | Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide |
title_full | Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide |
title_fullStr | Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide |
title_full_unstemmed | Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide |
title_short | Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide |
title_sort | surface plasmon resonance based biosensors for exploring the influence of alkaloids on aggregation of amyloid-β peptide |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3231330/ https://www.ncbi.nlm.nih.gov/pubmed/22163834 http://dx.doi.org/10.3390/s110404030 |
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