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Identification of a Prenyl Chalcone as a Competitive Lipoxygenase Inhibitor: Screening, Biochemical Evaluation and Molecular Modeling Studies
Cyclooxygenase (COX) and lipoxygenase (LOX) are key targets for the development of new anti-inflammatory agents. LOX, which is involved in the biosynthesis of mediators in inflammation and allergic reactions, was selected for a biochemical screening campaign to identify LOX inhibitors by employing t...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8069166/ https://www.ncbi.nlm.nih.gov/pubmed/33921198 http://dx.doi.org/10.3390/molecules26082205 |
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author | Zeraik, Maria Luiza Pauli, Ivani Dutra, Luiz A. Cruz, Raquel S. Valli, Marilia Paracatu, Luana C. de Faria, Carolina M. Q. G. Ximenes, Valdecir F. Regasini, Luis O. Andricopulo, Adriano D. Bolzani, Vanderlan S. |
author_facet | Zeraik, Maria Luiza Pauli, Ivani Dutra, Luiz A. Cruz, Raquel S. Valli, Marilia Paracatu, Luana C. de Faria, Carolina M. Q. G. Ximenes, Valdecir F. Regasini, Luis O. Andricopulo, Adriano D. Bolzani, Vanderlan S. |
author_sort | Zeraik, Maria Luiza |
collection | PubMed |
description | Cyclooxygenase (COX) and lipoxygenase (LOX) are key targets for the development of new anti-inflammatory agents. LOX, which is involved in the biosynthesis of mediators in inflammation and allergic reactions, was selected for a biochemical screening campaign to identify LOX inhibitors by employing the main natural product library of Brazilian biodiversity. Two prenyl chalcones were identified as potent inhibitors of LOX-1 in the screening. The most active compound, (E)-2-O-farnesyl chalcone, decreased the rate of oxygen consumption to an extent similar to that of the positive control, nordihydroguaiaretic acid. Additionally, studies on the mechanism of the action indicated that (E)-2-O-farnesyl chalcone is a competitive LOX-1 inhibitor. Molecular modeling studies indicated the importance of the prenyl moieties for the binding of the inhibitors to the LOX binding site, which is related to their pharmacological properties. |
format | Online Article Text |
id | pubmed-8069166 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-80691662021-04-26 Identification of a Prenyl Chalcone as a Competitive Lipoxygenase Inhibitor: Screening, Biochemical Evaluation and Molecular Modeling Studies Zeraik, Maria Luiza Pauli, Ivani Dutra, Luiz A. Cruz, Raquel S. Valli, Marilia Paracatu, Luana C. de Faria, Carolina M. Q. G. Ximenes, Valdecir F. Regasini, Luis O. Andricopulo, Adriano D. Bolzani, Vanderlan S. Molecules Article Cyclooxygenase (COX) and lipoxygenase (LOX) are key targets for the development of new anti-inflammatory agents. LOX, which is involved in the biosynthesis of mediators in inflammation and allergic reactions, was selected for a biochemical screening campaign to identify LOX inhibitors by employing the main natural product library of Brazilian biodiversity. Two prenyl chalcones were identified as potent inhibitors of LOX-1 in the screening. The most active compound, (E)-2-O-farnesyl chalcone, decreased the rate of oxygen consumption to an extent similar to that of the positive control, nordihydroguaiaretic acid. Additionally, studies on the mechanism of the action indicated that (E)-2-O-farnesyl chalcone is a competitive LOX-1 inhibitor. Molecular modeling studies indicated the importance of the prenyl moieties for the binding of the inhibitors to the LOX binding site, which is related to their pharmacological properties. MDPI 2021-04-12 /pmc/articles/PMC8069166/ /pubmed/33921198 http://dx.doi.org/10.3390/molecules26082205 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Zeraik, Maria Luiza Pauli, Ivani Dutra, Luiz A. Cruz, Raquel S. Valli, Marilia Paracatu, Luana C. de Faria, Carolina M. Q. G. Ximenes, Valdecir F. Regasini, Luis O. Andricopulo, Adriano D. Bolzani, Vanderlan S. Identification of a Prenyl Chalcone as a Competitive Lipoxygenase Inhibitor: Screening, Biochemical Evaluation and Molecular Modeling Studies |
title | Identification of a Prenyl Chalcone as a Competitive Lipoxygenase Inhibitor: Screening, Biochemical Evaluation and Molecular Modeling Studies |
title_full | Identification of a Prenyl Chalcone as a Competitive Lipoxygenase Inhibitor: Screening, Biochemical Evaluation and Molecular Modeling Studies |
title_fullStr | Identification of a Prenyl Chalcone as a Competitive Lipoxygenase Inhibitor: Screening, Biochemical Evaluation and Molecular Modeling Studies |
title_full_unstemmed | Identification of a Prenyl Chalcone as a Competitive Lipoxygenase Inhibitor: Screening, Biochemical Evaluation and Molecular Modeling Studies |
title_short | Identification of a Prenyl Chalcone as a Competitive Lipoxygenase Inhibitor: Screening, Biochemical Evaluation and Molecular Modeling Studies |
title_sort | identification of a prenyl chalcone as a competitive lipoxygenase inhibitor: screening, biochemical evaluation and molecular modeling studies |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8069166/ https://www.ncbi.nlm.nih.gov/pubmed/33921198 http://dx.doi.org/10.3390/molecules26082205 |
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