| Author | Menezes, Dayanne da Rocha de | |
| Author | Calvet, Claudia Magalhães | |
| Author | Rodrigues, Giseli Capaci | |
| Author | Pereira, Mirian Claudia de Souza | |
| Author | Almeida, Igor Rodrigues | |
| Author | Aguiar, Alcino Palermo de | |
| Author | Supuran, Claudiu T. | |
| Author | Vermelho, Alane Beatriz | |
| Access date | 2017-02-09T13:48:26Z | |
| Available date | 2017-02-09T13:48:26Z | |
| Document date | 2016 | |
| Citation | MENEZES, Dayanne da Rocha de; et al. Hydroxamic acid derivatives: a promising scaffold for rational compound optimization in Chagas disease. Journal of Enzyme Inhibition and Medicinal Chemistry, v.31, n.6, p.964-973, 2016. | pt_BR |
| ISSN | 1475-6366 | pt_BR |
| URI | https://www.arca.fiocruz.br/handle/icict/17769 | |
| Language | eng | pt_BR |
| Publisher | Taylor & Francis | pt_BR |
| Rights | restricted access | |
| Subject in Portuguese | Trypanosoma cruzi | pt_BR |
| Subject in Portuguese | Doença de Chagas | pt_BR |
| Subject in Portuguese | Derivados de ácido hidroxâmico | pt_BR |
| Title | Hydroxamic acid derivatives: a promising scaffold for rational compound optimization in Chagas disease | pt_BR |
| Type | Article | |
| DOI | 10.3109/14756366.2015.1077330 | |
| Abstract | This work describes the antitrypanocidal activity of two hydroxamic acid derivatives containing o-ethoxy (HAD1) and p-ethoxy (HAD2) as substituent in the aromatic ring linked to the isoxazoline ring. HAD1 and HAD2 induced a significant reduction in the number of intracellular parasites and consequently showed activity on the multiplication of the parasite. Treatment of cardiomyocytes and macrophages with the compounds revealed no significant loss in cell viability. Ultrastructural alterations after treatment of cardiomyocytes or macrophages infected by Trypanosoma cruzi with the IC50 value of HAD1 revealed alterations to amastigotes, showing initial damage seen as swelling of the kinetoplast. This gave a good indication of the ability of the drug to permeate through the host cell membrane as well as its selectivity to the parasite target. Both compounds HAD1 and 2 were able to reduce the cysteine peptidases and decrease the activity of metallopeptidases. | pt_BR |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Paulo de Góes. BIOINOVAR - Laboratórios de Biotecnologia: Biocatálise, Bioprodutos e Bioenergia. Rio de Janeiro, RJ, Brasil / Faculdade São Francisco de Barreiras (FASB). Barreiras, BA, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Ultra-estrutura Celular. Rio de Janeiro, RJ. Brasil. | pt_BR |
| Affilliation | Universidade do Grande Rio. Escola de Ciência e Tecnologia. Programa de Pós-Graduação em Ensino das Ciências. Duque de Caxias, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Ultra-estrutura Celular. Rio de Janeiro, RJ. Brasil. | pt_BR |
| Affilliation | Universidade Federal do Rio de Janeiro. Faculdade de Farmácia. Departamento de Produtos Naturais e Alimentos. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Instituto Militar de Engenharia. Departamento de Química. Laboratório de Síntese Orgãnica. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Universitá degli Studi di Firenzi. Polo Scientifico. Laboratorio di Chimica Bioinorganica. Sesto Fiorentino (Florence), Italy. | pt_BR |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Paulo de Góes. BIOINOVAR - Laboratórios de Biotecnologia: Biocatálise, Bioprodutos e Bioenergia. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Subject | Chagas disease | pt_BR |
| Subject | hydroxamic acid derivatives | pt_BR |
| Subject | Trypanosoma cruzi | pt_BR |
| e-ISSN | 1475-6374 | |
| Embargo date | 2030-01-01 | |
| xmlui.metadata.dc.subject.ods | 03 Saúde e Bem-Estar | |
