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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...

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Autores principales: Ferreira, Glaucio Monteiro, Kronenberger, Thales, de Almeida, Éryka Costa, Sampaio, Joseane, Terra, Clélia Ferreira, Pinto, Ernani, Trossini, Gustavo Henrique Goulart
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
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.
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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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