Secondary Metabolites in Ramalina terebrata Detected by UHPLC/ESI/MS/MS and Identification of Parietin as Tau Protein Inhibitor
Liquid chromatography coupled with mass spectrometry is an outstanding methodology for fast analysis of phenolic compounds in biological samples. Twenty two compounds were quickly and accurately identified in the methanolic extract of the Antarctic lichen Ramalina terebrata for the first time using...
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ftdoajarticles:oai:doaj.org/article:8dc9a73591784cd7a1dc3b39814b0df6 2023-05-15T13:55:29+02:00 Secondary Metabolites in Ramalina terebrata Detected by UHPLC/ESI/MS/MS and Identification of Parietin as Tau Protein Inhibitor Alberto Cornejo Francisco Salgado Julio Caballero Reinaldo Vargas Mario Simirgiotis Carlos Areche 2016-08-01T00:00:00Z https://doi.org/10.3390/ijms17081303 https://doaj.org/article/8dc9a73591784cd7a1dc3b39814b0df6 EN eng MDPI AG http://www.mdpi.com/1422-0067/17/8/1303 https://doaj.org/toc/1422-0067 1422-0067 doi:10.3390/ijms17081303 https://doaj.org/article/8dc9a73591784cd7a1dc3b39814b0df6 International Journal of Molecular Sciences, Vol 17, Iss 8, p 1303 (2016) Alzheimer’s disease docking Ramalina tau protein lichens parietin UHPLC/MS Biology (General) QH301-705.5 Chemistry QD1-999 article 2016 ftdoajarticles https://doi.org/10.3390/ijms17081303 2022-12-31T07:25:21Z Liquid chromatography coupled with mass spectrometry is an outstanding methodology for fast analysis of phenolic compounds in biological samples. Twenty two compounds were quickly and accurately identified in the methanolic extract of the Antarctic lichen Ramalina terebrata for the first time using ultra high pressure liquid chromatography coupled with photodiode array detector and high resolution mass spectrometry (UHPLC-PDA-Q/Orbitrap/MS/MS). In addition, the extract and the four compounds isolated from this species were tested for the inhibitory activity of tau protein aggregation, which is a protein involved in Alzheimer’s disease (AD). All compounds showed null activity with the exception of parietin, which it was able to inhibit aggregation process of tau in a concentration range between 3 µg/mL (10 µM) to 28 µg/mL (100 µM). In addition, we show how parietin interact with tau 306VQIVYK311 hexapeptide inside of the microtubule binding domain (4R) with the help of molecular docking experiments. Finally, the constituents present in the methanolic extract could possibly contribute to the established anti-aggregation activity for this extract and this in-depth analysis of the chemical composition of R. terebrata could guide further research into its medicinal properties and potential uses. Article in Journal/Newspaper Antarc* Antarctic Directory of Open Access Journals: DOAJ Articles Antarctic The Antarctic International Journal of Molecular Sciences 17 8 1303 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Alzheimer’s disease docking Ramalina tau protein lichens parietin UHPLC/MS Biology (General) QH301-705.5 Chemistry QD1-999 |
spellingShingle |
Alzheimer’s disease docking Ramalina tau protein lichens parietin UHPLC/MS Biology (General) QH301-705.5 Chemistry QD1-999 Alberto Cornejo Francisco Salgado Julio Caballero Reinaldo Vargas Mario Simirgiotis Carlos Areche Secondary Metabolites in Ramalina terebrata Detected by UHPLC/ESI/MS/MS and Identification of Parietin as Tau Protein Inhibitor |
topic_facet |
Alzheimer’s disease docking Ramalina tau protein lichens parietin UHPLC/MS Biology (General) QH301-705.5 Chemistry QD1-999 |
description |
Liquid chromatography coupled with mass spectrometry is an outstanding methodology for fast analysis of phenolic compounds in biological samples. Twenty two compounds were quickly and accurately identified in the methanolic extract of the Antarctic lichen Ramalina terebrata for the first time using ultra high pressure liquid chromatography coupled with photodiode array detector and high resolution mass spectrometry (UHPLC-PDA-Q/Orbitrap/MS/MS). In addition, the extract and the four compounds isolated from this species were tested for the inhibitory activity of tau protein aggregation, which is a protein involved in Alzheimer’s disease (AD). All compounds showed null activity with the exception of parietin, which it was able to inhibit aggregation process of tau in a concentration range between 3 µg/mL (10 µM) to 28 µg/mL (100 µM). In addition, we show how parietin interact with tau 306VQIVYK311 hexapeptide inside of the microtubule binding domain (4R) with the help of molecular docking experiments. Finally, the constituents present in the methanolic extract could possibly contribute to the established anti-aggregation activity for this extract and this in-depth analysis of the chemical composition of R. terebrata could guide further research into its medicinal properties and potential uses. |
format |
Article in Journal/Newspaper |
author |
Alberto Cornejo Francisco Salgado Julio Caballero Reinaldo Vargas Mario Simirgiotis Carlos Areche |
author_facet |
Alberto Cornejo Francisco Salgado Julio Caballero Reinaldo Vargas Mario Simirgiotis Carlos Areche |
author_sort |
Alberto Cornejo |
title |
Secondary Metabolites in Ramalina terebrata Detected by UHPLC/ESI/MS/MS and Identification of Parietin as Tau Protein Inhibitor |
title_short |
Secondary Metabolites in Ramalina terebrata Detected by UHPLC/ESI/MS/MS and Identification of Parietin as Tau Protein Inhibitor |
title_full |
Secondary Metabolites in Ramalina terebrata Detected by UHPLC/ESI/MS/MS and Identification of Parietin as Tau Protein Inhibitor |
title_fullStr |
Secondary Metabolites in Ramalina terebrata Detected by UHPLC/ESI/MS/MS and Identification of Parietin as Tau Protein Inhibitor |
title_full_unstemmed |
Secondary Metabolites in Ramalina terebrata Detected by UHPLC/ESI/MS/MS and Identification of Parietin as Tau Protein Inhibitor |
title_sort |
secondary metabolites in ramalina terebrata detected by uhplc/esi/ms/ms and identification of parietin as tau protein inhibitor |
publisher |
MDPI AG |
publishDate |
2016 |
url |
https://doi.org/10.3390/ijms17081303 https://doaj.org/article/8dc9a73591784cd7a1dc3b39814b0df6 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
International Journal of Molecular Sciences, Vol 17, Iss 8, p 1303 (2016) |
op_relation |
http://www.mdpi.com/1422-0067/17/8/1303 https://doaj.org/toc/1422-0067 1422-0067 doi:10.3390/ijms17081303 https://doaj.org/article/8dc9a73591784cd7a1dc3b39814b0df6 |
op_doi |
https://doi.org/10.3390/ijms17081303 |
container_title |
International Journal of Molecular Sciences |
container_volume |
17 |
container_issue |
8 |
container_start_page |
1303 |
_version_ |
1766262143958646784 |