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Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins
Aminopeptidase M (AMP) inhibition is of interest for several diseases, such as highly vascularized cancer types. AMP can be inhibited by linear pentapeptides isolated from Microcystis aeruginosa LTPNA08 (MG7XX). Porcine AMP inhibition—a model for human AMP—activity was spectrophotometrically measure...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6930480/ https://www.ncbi.nlm.nih.gov/pubmed/31795383 http://dx.doi.org/10.3390/molecules24234369 |
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author | Ferreira, Glaucio Monteiro Kronenberger, Thales de Almeida, Éryka Costa Sampaio, Joseane Terra, Clélia Ferreira Pinto, Ernani Trossini, Gustavo Henrique Goulart |
author_facet | Ferreira, Glaucio Monteiro Kronenberger, Thales de Almeida, Éryka Costa Sampaio, Joseane Terra, Clélia Ferreira Pinto, Ernani Trossini, Gustavo Henrique Goulart |
author_sort | Ferreira, Glaucio Monteiro |
collection | PubMed |
description | Aminopeptidase M (AMP) inhibition is of interest for several diseases, such as highly vascularized cancer types. AMP can be inhibited by linear pentapeptides isolated from Microcystis aeruginosa LTPNA08 (MG7XX). Porcine AMP inhibition—a model for human AMP—activity was spectrophotometrically measured by the formation of p-nitroanilide from L-leucine-p-nitroanilide substrate by AMP. AMP inhibition by MG770 exhibited comparable inhibition levels to amastatin (IC(50) values: 1.20 ± 0.1 μM and 0.98 ± 0.1 μM, respectively), while MG756 was slightly less potent (with IC(50) values of 3.26 ± 0.5 μM). Molecular modelling suggests a potential binding mode, based on the interaction with the Zn(2+) cofactor, where MG770′s extra methyl group contributes to the disturbance of the Zn(2+) cofactor complex and highlights the importance of hydrophobicity for the site. |
format | Online Article Text |
id | pubmed-6930480 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-69304802019-12-26 Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins Ferreira, Glaucio Monteiro Kronenberger, Thales de Almeida, Éryka Costa Sampaio, Joseane Terra, Clélia Ferreira Pinto, Ernani Trossini, Gustavo Henrique Goulart Molecules Article Aminopeptidase M (AMP) inhibition is of interest for several diseases, such as highly vascularized cancer types. AMP can be inhibited by linear pentapeptides isolated from Microcystis aeruginosa LTPNA08 (MG7XX). Porcine AMP inhibition—a model for human AMP—activity was spectrophotometrically measured by the formation of p-nitroanilide from L-leucine-p-nitroanilide substrate by AMP. AMP inhibition by MG770 exhibited comparable inhibition levels to amastatin (IC(50) values: 1.20 ± 0.1 μM and 0.98 ± 0.1 μM, respectively), while MG756 was slightly less potent (with IC(50) values of 3.26 ± 0.5 μM). Molecular modelling suggests a potential binding mode, based on the interaction with the Zn(2+) cofactor, where MG770′s extra methyl group contributes to the disturbance of the Zn(2+) cofactor complex and highlights the importance of hydrophobicity for the site. MDPI 2019-11-29 /pmc/articles/PMC6930480/ /pubmed/31795383 http://dx.doi.org/10.3390/molecules24234369 Text en © 2019 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Ferreira, Glaucio Monteiro Kronenberger, Thales de Almeida, Éryka Costa Sampaio, Joseane Terra, Clélia Ferreira Pinto, Ernani Trossini, Gustavo Henrique Goulart Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins |
title | Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins |
title_full | Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins |
title_fullStr | Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins |
title_full_unstemmed | Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins |
title_short | Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins |
title_sort | inhibition of porcine aminopeptidase m (pamp) by the pentapeptide microginins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6930480/ https://www.ncbi.nlm.nih.gov/pubmed/31795383 http://dx.doi.org/10.3390/molecules24234369 |
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