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dc.contributor.authorMelo, Ivna R.S.-
dc.contributor.authorDias, Lucas Pinheiro-
dc.contributor.authorAraújo, Nadine Monteiro Salgueiro-
dc.contributor.authorVasconcelos, Ilka Maria Aria-
dc.contributor.authorMartins, Thiago Fernandes-
dc.contributor.authorMorais, Glaucia Almeida de-
dc.contributor.authorGonçalves, José Francisco de Carvalho-
dc.contributor.authorNagano, C. S.-
dc.contributor.authorCarneiro, Rômulo F.-
dc.contributor.authorOliveira, José Tadeu A.Abreu-
dc.date.accessioned2020-06-15T21:35:33Z-
dc.date.available2020-06-15T21:35:33Z-
dc.date.issued2019-
dc.identifier.urihttps://repositorio.inpa.gov.br/handle/1/16642-
dc.description.abstractInfections caused by Candida tropicalis have increased significantly worldwide in parallel with resistance to antifungal drugs. To overcome resistance novel drugs have to be discovered. The objective of this work was to purify and characterize a cysteine protease inhibitor from the seeds of the Amazon rainforest tree Cassia leiandra and test its inhibitory effect against C. tropicalis growth. The inhibitor, named ClCPI, was purified after ion exchange and affinity chromatography followed by ultrafiltration. ClCPI is composed of a single polypeptide chain and is not a glycoprotein. The molecular mass determined by SDS-PAGE in the absence or presence of β-mercaptoethanol and ESI-MS were 16.63 kDa and 18.362 kDa, respectively. ClCPI was stable in the pH range of 7.0–9.0 and thermostable up to 60 °C for 20 min. ClCPI inhibited cysteine proteases, but not trypsin, chymotrypsin neither alpha-amylase. Inhibition of papain was uncompetitive with a Ki of 4.1 × 10 −7 M and IC 50 of 8.5 × 10 −7 M. ClCPI at 2.6 × 10 −6 M reduced 50% C. tropicalis growth. ClCPI induced damages and morphological alterations in C. tropicalis cell surface, which led to death. These results suggest that ClCPI have great potential for the development of an antifungal drug against C. tropicalis. © 2019en
dc.language.isoenpt_BR
dc.relation.ispartofVolume 133, Pags. 1115-1124pt_BR
dc.rightsRestrito*
dc.subjectAmylaseen
dc.subjectAntifungal Agenten
dc.subjectCassia Extracten
dc.subjectCassia Leiandra Extracten
dc.subjectChymotrypsinen
dc.subjectCysteine Proteinase Inhibitoren
dc.subjectMercaptoethanolen
dc.subjectPapainen
dc.subjectPolypeptideen
dc.subjectTrypsinen
dc.subjectUnclassified Drugen
dc.subjectAntifungal Agenten
dc.subjectCarbohydrateen
dc.subjectCysteine Proteinase Inhibitoren
dc.subjectReactive Oxygen Metaboliteen
dc.subjectThiol Derivativeen
dc.subjectChromatography, Affinityen
dc.subjectAmazonasen
dc.subjectAnti-fungal Activityen
dc.subjectCandida Tropicalisen
dc.subjectCassiaen
dc.subjectCassia Leiandraen
dc.subjectCell Deathen
dc.subjectCell Surfaceen
dc.subjectControlled Studyen
dc.subjectDrug Purificationen
dc.subjectDrug Stabilityen
dc.subjectElectrospray Mass Spectrometryen
dc.subjectEnzyme Inhibitionen
dc.subjectFungal Cellen
dc.subjectIc 50en
dc.subjectIon Exchange Chromatographyen
dc.subjectMolecular Weighten
dc.subjectNonhumanen
dc.subjectPhen
dc.subjectSeed Planten
dc.subjectElectrophoresis, Polyacrylamide Gelen
dc.subjectRainforesten
dc.subjectThermostabilityen
dc.subjectUltrafiltrationen
dc.subjectCandida Tropicalisen
dc.subjectCell Membrane Permeabilityen
dc.subjectChemistryen
dc.subjectCytologyen
dc.subjectDrug Effecten
dc.subjectMetabolismen
dc.subjectSeed Planten
dc.subjectTemperatureen
dc.subjectAntifungal Agentsen
dc.subjectCandida Tropicalisen
dc.subjectCarbohydratesen
dc.subjectCassiaen
dc.subjectCell Membrane Permeabilityen
dc.subjectCysteine Proteinase Inhibitorsen
dc.subjectHydrogen-ion Concentrationen
dc.subjectInhibitory Concentration 50en
dc.subjectMolecular Weighten
dc.subjectReactive Oxygen Speciesen
dc.subjectSeedsen
dc.subjectSulfhydryl Compoundsen
dc.subjectTemperatureen
dc.titleClCPI, a cysteine protease inhibitor purified from Cassia leiandra seeds has antifungal activity against Candida tropicalis by inducing disruption of the cell surfaceen
dc.typeArtigopt_BR
dc.identifier.doi10.1016/j.ijbiomac.2019.04.174-
dc.publisher.journalInternational Journal of Biological Macromoleculespt_BR
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