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Title: ClCPI, a cysteine protease inhibitor purified from Cassia leiandra seeds has antifungal activity against Candida tropicalis by inducing disruption of the cell surface
Authors: Melo, Ivna R.S.
Dias, Lucas Pinheiro
Araújo, Nadine Monteiro Salgueiro
Vasconcelos, Ilka Maria Aria
Martins, Thiago Fernandes
Morais, Glaucia Almeida de
Gonçalves, José Francisco de Carvalho
Nagano, C. S.
Carneiro, Rômulo F.
Oliveira, José Tadeu A.Abreu
Keywords: Amylase
Antifungal Agent
Cassia Extract
Cassia Leiandra Extract
Cysteine Proteinase Inhibitor
Unclassified Drug
Antifungal Agent
Cysteine Proteinase Inhibitor
Reactive Oxygen Metabolite
Thiol Derivative
Chromatography, Affinity
Anti-fungal Activity
Candida Tropicalis
Cassia Leiandra
Cell Death
Cell Surface
Controlled Study
Drug Purification
Drug Stability
Electrospray Mass Spectrometry
Enzyme Inhibition
Fungal Cell
Ic 50
Ion Exchange Chromatography
Molecular Weight
Seed Plant
Electrophoresis, Polyacrylamide Gel
Candida Tropicalis
Cell Membrane Permeability
Drug Effect
Seed Plant
Antifungal Agents
Candida Tropicalis
Cell Membrane Permeability
Cysteine Proteinase Inhibitors
Hydrogen-ion Concentration
Inhibitory Concentration 50
Molecular Weight
Reactive Oxygen Species
Sulfhydryl Compounds
Issue Date: 2019
metadata.dc.publisher.journal: International Journal of Biological Macromolecules
metadata.dc.relation.ispartof: Volume 133, Pags. 1115-1124
Abstract: Infections 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. © 2019
metadata.dc.identifier.doi: 10.1016/j.ijbiomac.2019.04.174
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