12 results on '"Teles, Carolina B. G."'
Search Results
2. Evaluation of sustainable susceptibility to Plasmodium vivax infection among colonized Anopheles darlingi and Anopheles deaneorum
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Santos, Najara A. C., Andrade, Alice O., Santos, Thais C., Martinez, Leandro N., Ferreira, Amália S., Bastos, Alessandra S., Martins, Mirilene M., Pontual, José D. C., Teles, Carolina B. G., Medeiros, Jansen F., and Araújo, Maisa S.
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- 2022
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3. Antileishmanial activity evaluation of a natural amide and its synthetic analogs against Leishmania (V.) braziliensis: an integrated approach in vitro and in silico
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da Silva, Minelly A., Fokoue, Harold H., Fialho, Saara N., dos Santos, Ana Paula de A., Rossi, Norton R. D. L. P., Gouveia, Aurileya de J., Ferreira, Amália S., Passarini, Guilherme M., Garay, Ana F. G., Alfonso, Jorge J., Soares, Andreimar M., Zanchi, Fernando B., Kato, Massuo J., Teles, Carolina B. G., and Kuehn, Christian C.
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- 2021
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4. Natural and Semisynthetic Triterpenes from Combretum leprosum Mart. with Antiplasmodial Activity
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Passarini, Guilherme M., Ferreira, Amália S., Moreira-Dill, Leandro S., Zanchi, Fernando B., Jesus, Aurileya G. de, Facundo, Valdir A., and Teles, Carolina B. G.
- Subjects
Plasmodium ,triterpenes ,antiplasmodial ,Combretum ,enoyl-reductase - Abstract
Malaria is responsible for thousands of deaths each year. Currently, artemisinin combination therapy (ACT) is used as first-choice medication against the disease. However, the emergence of resistant strains prompts the search for alternative compounds. The present study aimed to investigate the antiplasmodial activities of natural triterpenes (compounds 1 and 2), and semisynthetic derivatives 1a, 1b, 1c, and 1d. Antiplasmodial assays were carried out using the SYBR Green technique, whereas cytotoxicity was evaluated by the MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) method. Hemolytic assays were performed on human erythrocytes. An in silico analysis of the compounds against PfENR (Plasmodium falciparum 2-trans-enoyl-reductase) was carried out by molecular docking. Experiments with 1, and its derivatives against P. falciparum showed that 1a was very similar in terms of biological activity to compound 1 (half maximal inhibitory concentration (IC50) ca. 4 µM), whereas 1b, 1c, and 1d had reduced antiplasmodial activities (IC50 between 8-103 µM). The selectivity indexes of 1 and 1d for HepG2, and Vero cells were > 10. Docking results partially agreed with the in vitro experiments, with 1 and 1c having the best and worst affinities with PfENR, respectively. In conclusion, the results showed that 1 and 1d may serve as biotechnological tools in the development of antimalarial drugs.
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- 2022
5. Biochemical and Biological Profile of Parotoid Secretion of the Amazonian Rhinella marina (Anura: Bufonidae).
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Medeiros, Daniel S. S. de, Rego, Tiago B., Santos, Ana P. de A. dos, Pontes, Adriana S., Moreira-Dill, Leandro S., Matos, Najla B., Zuliani, Juliana P., Stábeli, Rodrigo G., Teles, Carolina B. G., Soares, Andreimar M., Sperotto, Angelo R. de M., Moura, Dinara J., Saffi, Jenifer, and Calderon, Leonardo A.
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PAROTID gland physiology ,POISON analysis ,ALKALOIDS ,ANURA ,BIOLOGICAL products ,ELECTROPHORESIS ,ESCHERICHIA coli ,LEISHMANIA ,LIQUID chromatography ,MASS spectrometry ,PROTOZOA ,PSEUDOMONAS ,SECRETION ,STAPHYLOCOCCUS aureus ,STEROIDS ,IN vivo studies - Abstract
Skin secretions of frogs have a high chemical complexity. They have diverse types of biomolecules, such as proteins, peptides, biogenic amines, and alkaloids. These compounds protect amphibians' skin against growth of bacteria, fungi, and protozoa and participate in defense system against attack from predators. Therewith, this work performed biochemical and biological profile of macroglands parotoid secretion from cane toad. For poison analysis, we performed molecular exclusion and reverse phase chromatography, electrophoresis, and mass spectrometry. Antimicrobial, antiplasmodial, leishmanicidal, cytotoxicity, genotoxicity, and inflammatory activity of crude and/or fractions of R. marina secretion were also evaluated. Fractionation prior to filtration from poison showed separation of low mass content (steroids and alkaloids) and high molecular mass (protein). Material below 10 kDa two steroids, marinobufagin and desacetylcinobufagin, was detected. Crude extract and fractions were active against Staphylococcus aureus, Pseudomonas aeruginosa, Escherichia coli, Plasmodium falciparum, Leishmania guyanensis, and Leishmania braziliensis. Crude extract was also active against cancer cells although it was not cytotoxic for normal cells. This extract did not show significant DNA damage but it showed an important inflammatory effect in vivo. The information obtained in this work contributes to the understanding of the constituents of R. marina secretion as well as the bioactive potential of these molecules. [ABSTRACT FROM AUTHOR]
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- 2019
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6. Corrigendum to “Biochemical and Biological Profile of Parotoid Secretion of the Amazonian Rhinella marina (Anura: Bufonidae)”.
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Medeiros, Daniel S. S. de, Rego, Tiago B., Santos, Ana P. de A. dos, Pontes, Adriana S., Moreira-Dill, Leandro S., Matos, Najla B., Zuliani, Juliana P., Stábeli, Rodrigo G., Teles, Carolina B. G., Soares, Andreimar M., Sperotto, Angelo R. de M., Moura, Dinara J., Saffi, Jenifer, Caldeira, Cleópatra Alves da Silva, Pimenta, Daniel Carvalho, and Calderon, Leonardo A.
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PAROTID gland physiology ,ANURA - Published
- 2019
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7. Synergism of in vitro plasmodicidal activity of phospholipase A2 isoforms isolated from panamanian Bothrops asper venom.
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Simões-Silva R, Alfonso JJ, Gómez AF, Sobrinho JC, Kayano AM, de Medeiros DSS, Teles CBG, Quintero A, Fuly AL, Gómez CV, Pereira SS, da Silva SL, Stábeli RG, and Soares AM
- Subjects
- Amino Acid Sequence, Animals, Antiprotozoal Agents chemistry, Antiprotozoal Agents isolation & purification, Bothrops metabolism, Drug Synergism, Isoelectric Point, Leishmania infantum drug effects, Panama, Parasitic Sensitivity Tests, Phospholipases A2 isolation & purification, Phospholipases A2 pharmacology, Protein Isoforms chemistry, Protein Isoforms isolation & purification, Protein Isoforms pharmacology, Sequence Alignment, Antiprotozoal Agents pharmacology, Phospholipases A2 chemistry, Plasmodium falciparum drug effects, Snake Venoms metabolism
- Abstract
Bothrops asper is one of the most important snake species in Central America, mainly because of its medical importance in countries like Ecuador, Panama and Costa Rica, where this species causes a high number of snakebite accidents. Several basic phospholipases A
2 (PLA2 s) have been previously characterized from B. asper venom, but few studies have been carried out with its acidic isoforms. In addition, since snake venom is a rich source of bioactive substances, it is necessary to investigate the biotechnological potential of its components. In this context, this study aimed to carry out the biochemical characterization of PLA2 isoforms isolated from B. asper venom and to evaluate the antiparasitic potential of these toxins. The venom and key fractions were subjected to different chromatographic steps, obtaining nine PLA2 s, four acidic ones (BaspAc-I, BaspAc-II, BaspAc-III and BaspAc-IV) and five basic ones (BaspB-I, BaspB-II, BaspB-III, BaspB-IV and BaspB-V). The isoelectric points of the acidic PLA2 s were also determined, which presented values ranging between 4.5 and 5. The findings indicated the isolation of five unpublished isoforms, four Asp49-PLA, corresponding to the group of acidic isoforms, and one Lys49-PLA2 -like. Acidic PLA2 s catalyzed the degradation of all substrates evaluated; however, for the basic PLA2 s, there was a preference for phosphatidylglycerol and phosphatidic acid. The antiparasitic potential of the toxins was evaluated, and the acidic PLA2 s demonstrated action against the epimastigote forms of T. cruzi and promastigote forms of L. infantum, while the basic PLA2 s BaspB-II and BaspB-IV showed activity against P. falciparum. The results indicated an increase of up to 10 times in antiplasmodial activity, when the Asp49-PLA2 and Lys49-PLA2 were associated with one another, denoting synergistic action between these PLA2 isoforms. These findings correspond to the first report of synergistic antiplasmodial action for svPLA2 s, demonstrating that these molecules may be important targets in the search for new antiparasitic agents., (Copyright © 2021 Elsevier B.V. All rights reserved.)- Published
- 2021
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8. Antimalarial activity of basic phospholipases A 2 isolated from Paraguayan Bothrops diporus venom against Plasmodium falciparum.
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Vitorino KA, Alfonso JJ, Gómez AF, Santos APA, Antunes YR, Caldeira CADS, Gómez CV, Teles CBG, Soares AM, and Calderon LA
- Abstract
Malaria is a parasitic infectious disease and was responsible for 400.000 deaths in 2018. Plasmodium falciparum represents the species that causes most human deaths due to severe malaria. In addition, studies prove the resistance of P. falciparum to drugs used to treat malaria, making the search for new drugs with antiplasmodial potential necessary. In this context, the literature describes snake venoms as a rich source of molecules with microbicidal potential, including phospholipases A
2 (PLA2 s). In this sense, the present study aimed to isolate basic PLA2 s from Paraguayan Bothrops diporus venom and evaluate their antiplasmodial potential. Basic PLA2 s were obtained using two chromatographic steps. Initially, B. diporus venom was subjected to ion exchange chromatography (IEC). The electrophoretic profile of the fractions from the IEC permitted the selection of 3 basic fractions, which were subjected to reverse phase chromatography, resulting in the isolation of the PLA2 s. The toxins were tested for enzymatic activity using a chromogenic substrate and finally, the antiplasmodial, cytotoxic potential and hemolytic activity of the isolated toxins were evaluated. The electrophoretic profile of the fractions from the IEC permitted the selection of 3 basic fractions, which were subjected to reverse phase chromatography, resulting in the isolation of the two enzymatically active PLA2 s, BdTX-I and BdTX-II and the PLA2 homologue BdTX-III. The antiplasmodial potential was evaluated and the toxins showed IC50 values of: 2.44, 0.0153 and 0.59 μg/mL respectively, presenting PLA2 selectivity according to the selectivity index results (SI) calculated against HepG2 cells. The results show that the 3 basic phospholipases isolated in this study have a potent antiparasitic effect against the W2 strain of P. falciparum . In view of the results obtained in this work, further research are necessary to determine the mechanism of action by which these toxins cause cell death in parasites., Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (© 2020 The Authors.)- Published
- 2020
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9. Corrigendum to "Biochemical and Biological Profile of Parotoid Secretion of the Amazonian Rhinella marina (Anura: Bufonidae)".
- Author
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de Medeiros DSS, Rego TB, Dos Santos APA, Pontes AS, Moreira-Dill LS, Matos NB, Zuliani JP, Stábeli RG, Teles CBG, Soares AM, Sperotto ARM, Moura DJ, Saffi J, Caldeira CADS, Pimenta DC, and Calderon LA
- Abstract
[This corrects the article DOI: 10.1155/2019/2492315.].
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- 2019
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10. Biochemical and Biological Profile of Parotoid Secretion of the Amazonian Rhinella marina (Anura: Bufonidae).
- Author
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de Medeiros DSS, Rego TB, Dos Santos APA, Pontes AS, Moreira-Dill LS, Matos NB, Zuliani JP, Stábeli RG, Teles CBG, Soares AM, Sperotto ARM, Moura DJ, Saffi J, Caldeira CADS, Pimenta DC, and Calderon LA
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- Animals, Bufo marinus, Anti-Bacterial Agents chemistry, Anti-Bacterial Agents metabolism, Anti-Bacterial Agents pharmacology, Bufanolides chemistry, Bufanolides metabolism, Bufanolides pharmacology, Parotid Gland metabolism, Pseudomonas aeruginosa growth & development, Skin metabolism, Staphylococcus aureus growth & development
- Abstract
Skin secretions of frogs have a high chemical complexity. They have diverse types of biomolecules, such as proteins, peptides, biogenic amines, and alkaloids. These compounds protect amphibians' skin against growth of bacteria, fungi, and protozoa and participate in defense system against attack from predators. Therewith, this work performed biochemical and biological profile of macroglands parotoid secretion from cane toad. For poison analysis, we performed molecular exclusion and reverse phase chromatography, electrophoresis, and mass spectrometry. Antimicrobial, antiplasmodial, leishmanicidal, cytotoxicity, genotoxicity, and inflammatory activity of crude and/or fractions of R. marina secretion were also evaluated. Fractionation prior to filtration from poison showed separation of low mass content (steroids and alkaloids) and high molecular mass (protein). Material below 10 kDa two steroids, marinobufagin and desacetylcinobufagin, was detected. Crude extract and fractions were active against Staphylococcus aureus , Pseudomonas aeruginosa , Escherichia coli , Plasmodium falciparum , Leishmania guyanensis , and Leishmania braziliensis . Crude extract was also active against cancer cells although it was not cytotoxic for normal cells. This extract did not show significant DNA damage but it showed an important inflammatory effect in vivo. The information obtained in this work contributes to the understanding of the constituents of R . marina secretion as well as the bioactive potential of these molecules.
- Published
- 2019
- Full Text
- View/download PDF
11. BmajPLA 2 -II, a basic Lys49-phospholipase A 2 homologue from Bothrops marajoensis snake venom with parasiticidal potential.
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Grabner AN, Alfonso J, Kayano AM, Moreira-Dill LS, Dos Santos APA, Caldeira CAS, Sobrinho JC, Gómez A, Grabner FP, Cardoso FF, Zuliani JP, Fontes MRM, Pimenta DC, Gómez CV, Teles CBG, Soares AM, and Calderon LA
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- Amino Acid Sequence, Animals, Antiprotozoal Agents metabolism, Phospholipases A2 metabolism, Trypsin metabolism, Antiprotozoal Agents chemistry, Antiprotozoal Agents pharmacology, Bothrops, Crotalid Venoms enzymology, Phospholipases A2 chemistry, Phospholipases A2 pharmacology, Sequence Homology, Amino Acid
- Abstract
Snake venoms contain various proteins, especially phospholipases A
2 (PLA2 s), which present potential applications in diverse areas of health and medicine. In this study, a new basic PLA2 from Bothrops marajoensis with parasiticidal activity was purified and characterized biochemically and biologically. B. marajoensis venom was fractionated through cation exchange followed by reverse phase chromatographies. The isolated toxin, BmajPLA2 -II, was structurally characterized with MALDI-TOF (Matrix-assisted laser desorption/ionization-time of flight) mass spectrometry, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), followed by two-dimensional electrophoresis, partial amino acid sequencing, an enzymatic activity assay, circular dichroism, and dynamic light scattering assays. These structural characterization tests presented BmajPLA2 -II as a basic Lys49 PLA2 homologue, compatible with other basic snake venom PLA2 s (svPLA2 ), with a tendency to form aggregations. The in vitro anti-parasitic potential of B. marajoensis venom and of BmajPLA2 -II was evaluated against Leishmania infantum promastigotes and Trypanosoma cruzi epimastigotes, showing significant activity at a concentration of 100μg/mL. The venom and BmajPLA2 -II presented IC50 of 0.14±0.08 and 6.41±0.64μg/mL, respectively, against intraerythrocytic forms of Plasmodium falciparum with CC50 cytotoxicity values against HepG2 cells of 43.64±7.94 and >150μg/mL, respectively. The biotechnological potential of these substances in relation to leishmaniasis, Chagas disease and malaria should be more deeply investigated., (Copyright © 2017. Published by Elsevier B.V.)- Published
- 2017
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12. Biological characterization of the Amazon coral Micrurus spixii snake venom: Isolation of a new neurotoxic phospholipase A2.
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Terra AL, Moreira-Dill LS, Simões-Silva R, Monteiro JR, Cavalcante WL, Gallacci M, Barros NB, Nicolete R, Teles CB, Medeiros PS, Zanchi FB, Zuliani JP, Calderon LA, Stábeli RG, and Soares AM
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- Amino Acid Sequence, Animals, Antiparasitic Agents pharmacology, Brazil, Creatine Kinase metabolism, Inhibitory Concentration 50, Leishmania drug effects, Leishmania growth & development, Mice, Molecular Sequence Data, Neurotoxins isolation & purification, Phospholipases A2 isolation & purification, Plasmodium falciparum drug effects, Plasmodium falciparum growth & development, Protein Conformation, Toxins, Biological, Elapid Venoms chemistry, Elapidae metabolism, Neurotoxins toxicity, Phospholipases A2 toxicity
- Abstract
The Micrurus genus is the American representative of Elapidae family. Micrurus spixii is endemic of South America and northern states of Brazil. Elapidic venoms contain neurotoxins that promote curare-mimetic neuromuscular blockage. In this study, biochemical and functional characterizations of M. spixii crude venom were performed and a new neurotoxic phospholipase A2 called MsPLA2-I was isolated. M. spixii crude venom caused severe swelling in the legs of tested mice and significant release of creatine kinase (CK) showing its myotoxic activity. Leishmanicidal activity against Leishmania amazonensis (IC50 1.24 μg/mL) was also observed, along with antiplasmodial activity against Plasmodium falciparum, which are unprecedented for Micrurus venoms. MsPLA2-I with a Mr 12,809.4 Da was isolated from the crude venom of M. spixii. The N-terminal sequencing of a fragment of 60 amino acids showed 80% similarity with another PLA2 from Micrurus altirostris. This toxin and the crude venom showed phospholipase activity. In a mouse phrenic nerve-diaphragm preparation, M. spixii venom and MsPLA2-I induced the blockage of both direct and indirect twitches. While the venom presented a pronounced myotoxic activity, MsPLA2-I expressed a summation of neurotoxic activity. The results of this study make M. spixii crude venom promising compounds in the exploration of molecules with microbicidal potential., (Copyright © 2015 Elsevier Ltd. All rights reserved.)
- Published
- 2015
- Full Text
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