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Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins

1
Department of Pharmacy, School of Pharmaceutical Sciences, University of São Paulo, Av Prof Lineu Prestes, 580, Bl. 13, São Paulo/SP CEP 05508-000, Brazil
2
Department of Oncology and Pneumology, Internal Medicine VIII, University Hospital Tübingen, Otfried-Müller-Straße 10, DE 72076 Tübingen, Germany
3
Department of Clinical and Toxicological Analyses, School of Pharmaceutical Sciences, University of São Paulo, Av Prof Lineu Prestes, 580, Bl. 17, São Paulo/SP CEP 05508-000, Brazil
4
Department of Biochemistry, Institute of Chemistry, University of São Paulo, Av Prof Lineu Prestes, 748, Bl. 12, São Paulo/SP CEP 05508-000, Brazil
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Molecules 2019, 24(23), 4369; https://doi.org/10.3390/molecules24234369
Received: 15 October 2019 / Revised: 11 November 2019 / Accepted: 12 November 2019 / Published: 29 November 2019
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 (IC50 values: 1.20 ± 0.1 μM and 0.98 ± 0.1 μM, respectively), while MG756 was slightly less potent (with IC50 values of 3.26 ± 0.5 μM). Molecular modelling suggests a potential binding mode, based on the interaction with the Zn2+ cofactor, where MG770′s extra methyl group contributes to the disturbance of the Zn2+ cofactor complex and highlights the importance of hydrophobicity for the site. View Full-Text
Keywords: aminopeptidase inhibition; cyanobacteria; Microcystis; microginin; molecular modelling aminopeptidase inhibition; cyanobacteria; Microcystis; microginin; molecular modelling
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Ferreira, G.M.; Kronenberger, T.; de Almeida, É.C.; Sampaio, J.; Terra, C.F.; Pinto, E.; Trossini, G.H.G. Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins. Molecules 2019, 24, 4369.

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