Cargando…
Evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure–activity relationship
α-Amylase has been considered an important therapeutic target for the management of type 2 diabetes mellitus (T2DM), decreasing postprandial hyperglycaemia (PPHG). In the present work, a panel of 40 structurally related flavonoids was tested, concerning their ability to inhibit α-amylase activity, u...
Autores principales: | , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6366418/ https://www.ncbi.nlm.nih.gov/pubmed/30724629 http://dx.doi.org/10.1080/14756366.2018.1558221 |
_version_ | 1783393622827204608 |
---|---|
author | Proença, Carina Freitas, Marisa Ribeiro, Daniela Tomé, Sara M. Oliveira, Eduardo F. T. Viegas, Matilde F. Araújo, Alberto N. Ramos, Maria J. Silva, Artur M. S. Fernandes, Pedro A. Fernandes, Eduarda |
author_facet | Proença, Carina Freitas, Marisa Ribeiro, Daniela Tomé, Sara M. Oliveira, Eduardo F. T. Viegas, Matilde F. Araújo, Alberto N. Ramos, Maria J. Silva, Artur M. S. Fernandes, Pedro A. Fernandes, Eduarda |
author_sort | Proença, Carina |
collection | PubMed |
description | α-Amylase has been considered an important therapeutic target for the management of type 2 diabetes mellitus (T2DM), decreasing postprandial hyperglycaemia (PPHG). In the present work, a panel of 40 structurally related flavonoids was tested, concerning their ability to inhibit α-amylase activity, using a microanalysis screening system, an inhibitory kinetic analysis and molecular docking calculations. From the obtained results, it was possible to observe that the flavone with a -Cl ion at 3-position of C-ring, an –OH group at 3′- and 4′- positions of B-ring and at 5- and 7- positions of A-ring and the C2 = C3 double bond, was the most active tested flavonoid, through competitive inhibition. In conclusion, some of the tested flavonoids have shown promising inhibition of α-amylase and may be considered as possible alternatives to the modulation of T2DM. |
format | Online Article Text |
id | pubmed-6366418 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-63664182019-02-15 Evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure–activity relationship Proença, Carina Freitas, Marisa Ribeiro, Daniela Tomé, Sara M. Oliveira, Eduardo F. T. Viegas, Matilde F. Araújo, Alberto N. Ramos, Maria J. Silva, Artur M. S. Fernandes, Pedro A. Fernandes, Eduarda J Enzyme Inhib Med Chem Article α-Amylase has been considered an important therapeutic target for the management of type 2 diabetes mellitus (T2DM), decreasing postprandial hyperglycaemia (PPHG). In the present work, a panel of 40 structurally related flavonoids was tested, concerning their ability to inhibit α-amylase activity, using a microanalysis screening system, an inhibitory kinetic analysis and molecular docking calculations. From the obtained results, it was possible to observe that the flavone with a -Cl ion at 3-position of C-ring, an –OH group at 3′- and 4′- positions of B-ring and at 5- and 7- positions of A-ring and the C2 = C3 double bond, was the most active tested flavonoid, through competitive inhibition. In conclusion, some of the tested flavonoids have shown promising inhibition of α-amylase and may be considered as possible alternatives to the modulation of T2DM. Taylor & Francis 2019-02-06 /pmc/articles/PMC6366418/ /pubmed/30724629 http://dx.doi.org/10.1080/14756366.2018.1558221 Text en © 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Article Proença, Carina Freitas, Marisa Ribeiro, Daniela Tomé, Sara M. Oliveira, Eduardo F. T. Viegas, Matilde F. Araújo, Alberto N. Ramos, Maria J. Silva, Artur M. S. Fernandes, Pedro A. Fernandes, Eduarda Evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure–activity relationship |
title | Evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure–activity relationship |
title_full | Evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure–activity relationship |
title_fullStr | Evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure–activity relationship |
title_full_unstemmed | Evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure–activity relationship |
title_short | Evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure–activity relationship |
title_sort | evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure–activity relationship |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6366418/ https://www.ncbi.nlm.nih.gov/pubmed/30724629 http://dx.doi.org/10.1080/14756366.2018.1558221 |
work_keys_str_mv | AT proencacarina evaluationofaflavonoidslibraryforinhibitionofpancreaticaamylasetowardsastructureactivityrelationship AT freitasmarisa evaluationofaflavonoidslibraryforinhibitionofpancreaticaamylasetowardsastructureactivityrelationship AT ribeirodaniela evaluationofaflavonoidslibraryforinhibitionofpancreaticaamylasetowardsastructureactivityrelationship AT tomesaram evaluationofaflavonoidslibraryforinhibitionofpancreaticaamylasetowardsastructureactivityrelationship AT oliveiraeduardoft evaluationofaflavonoidslibraryforinhibitionofpancreaticaamylasetowardsastructureactivityrelationship AT viegasmatildef evaluationofaflavonoidslibraryforinhibitionofpancreaticaamylasetowardsastructureactivityrelationship AT araujoalberton evaluationofaflavonoidslibraryforinhibitionofpancreaticaamylasetowardsastructureactivityrelationship AT ramosmariaj evaluationofaflavonoidslibraryforinhibitionofpancreaticaamylasetowardsastructureactivityrelationship AT silvaarturms evaluationofaflavonoidslibraryforinhibitionofpancreaticaamylasetowardsastructureactivityrelationship AT fernandespedroa evaluationofaflavonoidslibraryforinhibitionofpancreaticaamylasetowardsastructureactivityrelationship AT fernandeseduarda evaluationofaflavonoidslibraryforinhibitionofpancreaticaamylasetowardsastructureactivityrelationship |