ClCPI, a cysteine protease inhibitor purified from Cassia leiandra seeds has antifungal activity against Candida tropicalis by inducing disruption of the cell surface
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 Amaz...
| Autor principal: | Melo, Ivna R.S. |
|---|---|
| Outros Autores: | Dias, Lucas Pinheiro, Araújo, Nadine Monteiro Salgueiro, Vasconcelos, Ilka Maria Aria, Martins, Thiago Fernandes, Morais, Glaucia Almeida de, Gonçalves, José Francisco Carvalho de, Nagano, C. S., Carneiro, Rômulo F., Oliveira, José Tadeu A.Abreu |
| Grau: | Artigo |
| Idioma: | English |
| Publicado em: |
International Journal of Biological Macromolecules
2020
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| Acesso em linha: |
https://repositorio.inpa.gov.br/handle/1/16642 |
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oai:repositorio:1-16642 |
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oai:repositorio:1-16642 ClCPI, a cysteine protease inhibitor purified from Cassia leiandra seeds has antifungal activity against Candida tropicalis by inducing disruption of the cell surface 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 Carvalho de Nagano, C. S. Carneiro, Rômulo F. Oliveira, José Tadeu A.Abreu Amylase Antifungal Agent Cassia Extract Cassia Leiandra Extract Chymotrypsin Cysteine Proteinase Inhibitor Mercaptoethanol Papain Polypeptide Trypsin Unclassified Drug Antifungal Agent Carbohydrate Cysteine Proteinase Inhibitor Reactive Oxygen Metabolite Thiol Derivative Chromatography, Affinity Amazonas Anti-fungal Activity Candida Tropicalis Cassia 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 Nonhuman Ph Seed Plant Electrophoresis, Polyacrylamide Gel Rainforest Thermostability Ultrafiltration Candida Tropicalis Cell Membrane Permeability Chemistry Cytology Drug Effect Metabolism Seed Plant Temperature Antifungal Agents Candida Tropicalis Carbohydrates Cassia Cell Membrane Permeability Cysteine Proteinase Inhibitors Hydrogen-ion Concentration Inhibitory Concentration 50 Molecular Weight Reactive Oxygen Species Seeds Sulfhydryl Compounds Temperature 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 2020-06-15T21:35:33Z 2020-06-15T21:35:33Z 2019 Artigo https://repositorio.inpa.gov.br/handle/1/16642 10.1016/j.ijbiomac.2019.04.174 en Volume 133, Pags. 1115-1124 Restrito International Journal of Biological Macromolecules |
| institution |
Instituto Nacional de Pesquisas da Amazônia - Repositório Institucional |
| collection |
INPA-RI |
| language |
English |
| topic |
Amylase Antifungal Agent Cassia Extract Cassia Leiandra Extract Chymotrypsin Cysteine Proteinase Inhibitor Mercaptoethanol Papain Polypeptide Trypsin Unclassified Drug Antifungal Agent Carbohydrate Cysteine Proteinase Inhibitor Reactive Oxygen Metabolite Thiol Derivative Chromatography, Affinity Amazonas Anti-fungal Activity Candida Tropicalis Cassia 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 Nonhuman Ph Seed Plant Electrophoresis, Polyacrylamide Gel Rainforest Thermostability Ultrafiltration Candida Tropicalis Cell Membrane Permeability Chemistry Cytology Drug Effect Metabolism Seed Plant Temperature Antifungal Agents Candida Tropicalis Carbohydrates Cassia Cell Membrane Permeability Cysteine Proteinase Inhibitors Hydrogen-ion Concentration Inhibitory Concentration 50 Molecular Weight Reactive Oxygen Species Seeds Sulfhydryl Compounds Temperature |
| spellingShingle |
Amylase Antifungal Agent Cassia Extract Cassia Leiandra Extract Chymotrypsin Cysteine Proteinase Inhibitor Mercaptoethanol Papain Polypeptide Trypsin Unclassified Drug Antifungal Agent Carbohydrate Cysteine Proteinase Inhibitor Reactive Oxygen Metabolite Thiol Derivative Chromatography, Affinity Amazonas Anti-fungal Activity Candida Tropicalis Cassia 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 Nonhuman Ph Seed Plant Electrophoresis, Polyacrylamide Gel Rainforest Thermostability Ultrafiltration Candida Tropicalis Cell Membrane Permeability Chemistry Cytology Drug Effect Metabolism Seed Plant Temperature Antifungal Agents Candida Tropicalis Carbohydrates Cassia Cell Membrane Permeability Cysteine Proteinase Inhibitors Hydrogen-ion Concentration Inhibitory Concentration 50 Molecular Weight Reactive Oxygen Species Seeds Sulfhydryl Compounds Temperature Melo, Ivna R.S. ClCPI, a cysteine protease inhibitor purified from Cassia leiandra seeds has antifungal activity against Candida tropicalis by inducing disruption of the cell surface |
| topic_facet |
Amylase Antifungal Agent Cassia Extract Cassia Leiandra Extract Chymotrypsin Cysteine Proteinase Inhibitor Mercaptoethanol Papain Polypeptide Trypsin Unclassified Drug Antifungal Agent Carbohydrate Cysteine Proteinase Inhibitor Reactive Oxygen Metabolite Thiol Derivative Chromatography, Affinity Amazonas Anti-fungal Activity Candida Tropicalis Cassia 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 Nonhuman Ph Seed Plant Electrophoresis, Polyacrylamide Gel Rainforest Thermostability Ultrafiltration Candida Tropicalis Cell Membrane Permeability Chemistry Cytology Drug Effect Metabolism Seed Plant Temperature Antifungal Agents Candida Tropicalis Carbohydrates Cassia Cell Membrane Permeability Cysteine Proteinase Inhibitors Hydrogen-ion Concentration Inhibitory Concentration 50 Molecular Weight Reactive Oxygen Species Seeds Sulfhydryl Compounds Temperature |
| description |
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 |
| format |
Artigo |
| author |
Melo, Ivna R.S. |
| author2 |
Dias, Lucas Pinheiro Araújo, Nadine Monteiro Salgueiro Vasconcelos, Ilka Maria Aria Martins, Thiago Fernandes Morais, Glaucia Almeida de Gonçalves, José Francisco Carvalho de Nagano, C. S. Carneiro, Rômulo F. Oliveira, José Tadeu A.Abreu |
| author2Str |
Dias, Lucas Pinheiro Araújo, Nadine Monteiro Salgueiro Vasconcelos, Ilka Maria Aria Martins, Thiago Fernandes Morais, Glaucia Almeida de Gonçalves, José Francisco Carvalho de Nagano, C. S. Carneiro, Rômulo F. Oliveira, José Tadeu A.Abreu |
| title |
ClCPI, a cysteine protease inhibitor purified from Cassia leiandra seeds has antifungal activity against Candida tropicalis by inducing disruption of the cell surface |
| title_short |
ClCPI, a cysteine protease inhibitor purified from Cassia leiandra seeds has antifungal activity against Candida tropicalis by inducing disruption of the cell surface |
| title_full |
ClCPI, a cysteine protease inhibitor purified from Cassia leiandra seeds has antifungal activity against Candida tropicalis by inducing disruption of the cell surface |
| title_fullStr |
ClCPI, a cysteine protease inhibitor purified from Cassia leiandra seeds has antifungal activity against Candida tropicalis by inducing disruption of the cell surface |
| title_full_unstemmed |
ClCPI, a cysteine protease inhibitor purified from Cassia leiandra seeds has antifungal activity against Candida tropicalis by inducing disruption of the cell surface |
| title_sort |
clcpi, a cysteine protease inhibitor purified from cassia leiandra seeds has antifungal activity against candida tropicalis by inducing disruption of the cell surface |
| publisher |
International Journal of Biological Macromolecules |
| publishDate |
2020 |
| url |
https://repositorio.inpa.gov.br/handle/1/16642 |
| _version_ |
1787145075477708800 |
| score |
11.755432 |