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Amyloid Aggregation of Insulin: An Interaction Study of Green Tea Constituents
Exogenous insulin, used as a therapeutic agent for diabetes, forms insoluble deposits containing amyloid fibrillar structures near the administration site. We have analyzed the in vitro anti-amyloid activity of four green tea constituents: (-)-epigallocatechin gallate (EGCG), (-)-epicatechin (EC), g...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7272432/ https://www.ncbi.nlm.nih.gov/pubmed/32499589 http://dx.doi.org/10.1038/s41598-020-66033-6 |
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author | Gancar, Miroslav Kurin, Elena Bednarikova, Zuzana Marek, Jozef Mucaji, Pavel Nagy, Milan Gazova, Zuzana |
author_facet | Gancar, Miroslav Kurin, Elena Bednarikova, Zuzana Marek, Jozef Mucaji, Pavel Nagy, Milan Gazova, Zuzana |
author_sort | Gancar, Miroslav |
collection | PubMed |
description | Exogenous insulin, used as a therapeutic agent for diabetes, forms insoluble deposits containing amyloid fibrillar structures near the administration site. We have analyzed the in vitro anti-amyloid activity of four green tea constituents: (-)-epigallocatechin gallate (EGCG), (-)-epicatechin (EC), gallic acid (GA), caffeine (CF), and their equimolar mixtures. Regarding individually tested compounds, only EGCG inhibited the fibrillization process. The individual EC, GA, and CF molecules were ineffective. The presence of EGCG in equimolar combinations with GA, EC, or CF was required for the inhibitory activity of most mixtures. Molecular docking revealed that EGCG interacts with an essential amyloidogenic region of insulin chain B. Individually inactive GA had a potentiating effect on the activity of EGCG. In contrast, EC and CF had a negative impact on the activity of the mixtures. We have observed diverse morphology and the amount of insulin amyloid aggregates formed in the presence of studied compounds. The distinct types of amyloid aggregates created in vitro in the presence of EGCG and other green tea constituents were characterized. Results indicate that the biological activity of individual molecules is not directly applicable to the pooled samples effects prediction. |
format | Online Article Text |
id | pubmed-7272432 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-72724322020-06-05 Amyloid Aggregation of Insulin: An Interaction Study of Green Tea Constituents Gancar, Miroslav Kurin, Elena Bednarikova, Zuzana Marek, Jozef Mucaji, Pavel Nagy, Milan Gazova, Zuzana Sci Rep Article Exogenous insulin, used as a therapeutic agent for diabetes, forms insoluble deposits containing amyloid fibrillar structures near the administration site. We have analyzed the in vitro anti-amyloid activity of four green tea constituents: (-)-epigallocatechin gallate (EGCG), (-)-epicatechin (EC), gallic acid (GA), caffeine (CF), and their equimolar mixtures. Regarding individually tested compounds, only EGCG inhibited the fibrillization process. The individual EC, GA, and CF molecules were ineffective. The presence of EGCG in equimolar combinations with GA, EC, or CF was required for the inhibitory activity of most mixtures. Molecular docking revealed that EGCG interacts with an essential amyloidogenic region of insulin chain B. Individually inactive GA had a potentiating effect on the activity of EGCG. In contrast, EC and CF had a negative impact on the activity of the mixtures. We have observed diverse morphology and the amount of insulin amyloid aggregates formed in the presence of studied compounds. The distinct types of amyloid aggregates created in vitro in the presence of EGCG and other green tea constituents were characterized. Results indicate that the biological activity of individual molecules is not directly applicable to the pooled samples effects prediction. Nature Publishing Group UK 2020-06-04 /pmc/articles/PMC7272432/ /pubmed/32499589 http://dx.doi.org/10.1038/s41598-020-66033-6 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Gancar, Miroslav Kurin, Elena Bednarikova, Zuzana Marek, Jozef Mucaji, Pavel Nagy, Milan Gazova, Zuzana Amyloid Aggregation of Insulin: An Interaction Study of Green Tea Constituents |
title | Amyloid Aggregation of Insulin: An Interaction Study of Green Tea Constituents |
title_full | Amyloid Aggregation of Insulin: An Interaction Study of Green Tea Constituents |
title_fullStr | Amyloid Aggregation of Insulin: An Interaction Study of Green Tea Constituents |
title_full_unstemmed | Amyloid Aggregation of Insulin: An Interaction Study of Green Tea Constituents |
title_short | Amyloid Aggregation of Insulin: An Interaction Study of Green Tea Constituents |
title_sort | amyloid aggregation of insulin: an interaction study of green tea constituents |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7272432/ https://www.ncbi.nlm.nih.gov/pubmed/32499589 http://dx.doi.org/10.1038/s41598-020-66033-6 |
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