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Doctoral Thesis
DOI
https://doi.org/10.11606/T.42.2017.tde-02102017-162349
Document
Author
Full name
Jasmin Lindner
Institute/School/College
Knowledge Area
Date of Defense
Published
São Paulo, 2017
Supervisor
Committee
Wrenger, Carsten (President)
Albrecht, Letusa
Palmisano, Giuseppe
Tonelli, Renata Rosito
Title in Portuguese
Análise do catabolismo da hemoglobina de Plasmodium falciparum.
Keywords in Portuguese
Plasmodium falciparum
Anemia falciforme
Hemoglobina
Protease
Abstract in Portuguese
O metabolismo de nutrientes abriga um alto potencial para o desenvolvimento de novos alvos quimioterápicos para o tratamento do parasita da malária Plasmodium falciparum. A partir de ensaios de crescimento do parasita dentro de eritrócitos geneticamente diferentes, concentrando-se na via catabólica da hemoglobina plasmodial usando parasitas transgênicos, a natureza protetora das variantes da hemoglobina foi investigada. Sendo que Falcipain 2 (FP2) prolifera três vezes mais elevada no sangue de células falciformes do que o Mock, a célula de controle. Adicionalmente, estudos de inibidores indicam que FP2 é uma proteína essencial para o parasita. Em cooperação com o DESY em Hamburgo, Alemanha a estrutura cristalina da amino peptidase P foi resolvida difratando até 1,7 Å.
Title in English
Analysis of the haemoglobin catabolism of Plasmodium falciparum.
Keywords in English
Plasmodium falciparum
haemoglobin
protease
sickle cell trait
Abstract in English
The metabolism of nutrients harbors a high potential for the development of new chemotherapeutic targets for the treatment of the malaria parasite Plasmodium falciparum. From parasite growth assays within genetically different erythrocytes, concentrating on the catabolic pathway of plasmodial hemoglobin using transgenic parasites, the protective nature of hemoglobin variants was investigated. Since Falcipain 2 (FP2) proliferates three times higher in sickle cell blood than the Mock, the control cell. In addition, inhibitor studies indicate that FP2 is an essential protein for the parasite. In cooperation with DESY in Hamburg, Germany the crystalline structure of the amino peptidase P was resolved diffracting up to 1.7 Å.
 
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Publishing Date
2017-10-02
 
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