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A fast, miniaturised in-vitro assay developed for quantification of lipase enzyme activity
The discovery of allosteric modulators is a multi-disciplinary approach, which is time- and cost-intensive. High-throughput screening combined with novel computational tools can reduce these factors. Thus, we developed an enzyme activity assay, which can be included in the drug discovery work-flow s...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6713963/ https://www.ncbi.nlm.nih.gov/pubmed/31414611 http://dx.doi.org/10.1080/14756366.2019.1651312 |
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author | Menden, Ariane Hall, Davane Paris, Daniel Mathura, Venkatarian Crawford, Fiona Mullan, Michael Crynen, Stefan Ait-Ghezala, Ghania |
author_facet | Menden, Ariane Hall, Davane Paris, Daniel Mathura, Venkatarian Crawford, Fiona Mullan, Michael Crynen, Stefan Ait-Ghezala, Ghania |
author_sort | Menden, Ariane |
collection | PubMed |
description | The discovery of allosteric modulators is a multi-disciplinary approach, which is time- and cost-intensive. High-throughput screening combined with novel computational tools can reduce these factors. Thus, we developed an enzyme activity assay, which can be included in the drug discovery work-flow subsequent to the in-silico library screening. While the in-silico screening yields in the identification of potential allosteric modulators, the developed in-vitro assay allows for the characterisation of them. Candida rugosa lipase (CRL), a glyceride hydrolysing enzyme, has been selected for the pilot development. The assay conditions were adjusted to CRL’s properties including pH, temperature and substrate specificity for two different substrates. The optimised assay conditions were validated and were used to characterise Tropolone, which was identified as an allosteric modulator. In conclusion, the assay is a reliable, reproducible, and robust tool, which can be streamlined with in-silico screening and incorporated in an automated high-throughput screening workflow. |
format | Online Article Text |
id | pubmed-6713963 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-67139632019-09-06 A fast, miniaturised in-vitro assay developed for quantification of lipase enzyme activity Menden, Ariane Hall, Davane Paris, Daniel Mathura, Venkatarian Crawford, Fiona Mullan, Michael Crynen, Stefan Ait-Ghezala, Ghania J Enzyme Inhib Med Chem Research Paper The discovery of allosteric modulators is a multi-disciplinary approach, which is time- and cost-intensive. High-throughput screening combined with novel computational tools can reduce these factors. Thus, we developed an enzyme activity assay, which can be included in the drug discovery work-flow subsequent to the in-silico library screening. While the in-silico screening yields in the identification of potential allosteric modulators, the developed in-vitro assay allows for the characterisation of them. Candida rugosa lipase (CRL), a glyceride hydrolysing enzyme, has been selected for the pilot development. The assay conditions were adjusted to CRL’s properties including pH, temperature and substrate specificity for two different substrates. The optimised assay conditions were validated and were used to characterise Tropolone, which was identified as an allosteric modulator. In conclusion, the assay is a reliable, reproducible, and robust tool, which can be streamlined with in-silico screening and incorporated in an automated high-throughput screening workflow. Taylor & Francis 2019-08-15 /pmc/articles/PMC6713963/ /pubmed/31414611 http://dx.doi.org/10.1080/14756366.2019.1651312 Text en © 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Menden, Ariane Hall, Davane Paris, Daniel Mathura, Venkatarian Crawford, Fiona Mullan, Michael Crynen, Stefan Ait-Ghezala, Ghania A fast, miniaturised in-vitro assay developed for quantification of lipase enzyme activity |
title | A fast, miniaturised in-vitro assay developed for
quantification of lipase enzyme activity |
title_full | A fast, miniaturised in-vitro assay developed for
quantification of lipase enzyme activity |
title_fullStr | A fast, miniaturised in-vitro assay developed for
quantification of lipase enzyme activity |
title_full_unstemmed | A fast, miniaturised in-vitro assay developed for
quantification of lipase enzyme activity |
title_short | A fast, miniaturised in-vitro assay developed for
quantification of lipase enzyme activity |
title_sort | fast, miniaturised in-vitro assay developed for
quantification of lipase enzyme activity |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6713963/ https://www.ncbi.nlm.nih.gov/pubmed/31414611 http://dx.doi.org/10.1080/14756366.2019.1651312 |
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