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Previous issue date: 2009-02-06 / Chitin is an important structural component of the cellular wall of fungi and exoskeleton of many invertebrate plagues, such as insects and nematodes. In digestory systems of insects it forms a named matrix of peritrophic membrane. One of the most studied interaction models protein-carbohydrate is the model that involves chitin-binding proteins. Among the involved characterized domains already in this interaction if they detach the hevein domain (HD), from of Hevea brasiliensis (Rubber tree), the R&R consensus domain (R&R), found in cuticular proteins of insects, and the motif called in this study as conglicinin motif (CD), found in the cristallography structure of the β-conglicinin bounded with GlcNac. These three chitin-binding domains had been used to determine which of them could be involved in silico in the interaction of Canavalia ensiformis and Vigna unguiculata vicilins with chitin, as well as associate these results with the WD50 of these vicilins for Callosobruchus maculatus larvae. The technique of comparative modeling was used for construction of the model 3D of the vicilin of V. unguiculata, that was not found in the data bases. Using the ClustalW program it was gotten localization of these domains in the vicilins primary structure. The domains R&R and CD had been found with bigger homology in the vicilins primary sequences and had been target of interaction studies. Through program GRAMM models of interaction ( dockings ) of the vicilins with GlcNac had been gotten. The results had shown that, through analysis in silico, HD is not part of the vicilins structures, proving the result gotten with the alignment of the primary sequences; the R&R domain, although not to have structural similarity in the vicilins, probably it has a participation in the activity of interaction of these with GlcNac; whereas the CD domain participates directly in the interaction of the vicilins with GlcNac. These results in silico show that the amino acid number, the types and the amount of binding made for the CD motif with GlcNac seem to be directly associates to the deleterious power that these vicilins show for C. maculatus larvae. This can give an initial step in the briefing of as the vicilins interact with alive chitin in and exert its toxic power for insects that possess peritrophic membrane / A quitina (homopol?mero linear contendo res?duos de β-1,4-N-acetil-D-glicosamina (GlcNac) ? um importante componente estrutural da parede celular de fungos e exoesqueletos de muitos invertebrados pragas, tais como insetos e nemat?ides. Em sistemas digest?rios de insetos forma uma matriz denominada de membrana peritr?fica. Um dos mais estudados modelos de intera??o prote?na-carboidrato ? o modelo que envolve as prote?nas ligantes ? quitina. Dentre os motivos j? caracterizados envolvidos nesta intera??o se destacam o motivo heve?na (HD), obtida de Hevea brasiliensis (Seringueira), o motivo R&R consenso (R&R), encontrado em prote?nas cuticulares de insetos, e o motivo denominado neste estudo como motivo conglicinina (CD), encontrado na estrutura cristalogr?fica da β-conglicinina complexada com GlcNac. Estes tr?s motivos de liga??o ? quitina foram usados para determinar qual(is) deles poderia(m) estar envolvido(s) in silico na intera??o das vicilinas de Canavalia ensiformis e Vigna unguiculata com quitina, como tamb?m associar estes resultados com o WD50 destas vicilinas para larvas de Callosobruchus maculatus. A t?cnica de modelagem comparativa foi utilizada para constru??o do modelo 3D da vicilina de V. unguiculata, que n?o foi encontrada nos bancos de dados. Atrav?s do programa ClustalW obteve-se a localiza??o destes dom?nios na estrutura prim?ria das vicilinas. Os dom?nios R&R e CD foram encontrados com maior homologia nas seq??ncias prim?rias das vicilinas e foram alvos de estudos de intera??o. Atrav?s do programa GRAMM foram obtidos modelos de intera??o ( dockings ) das vicilinas com GlcNac. Os resultados mostraram que, atrav?s de an?lises in silico, o motivo HD n?o faz parte da estrutura das vicilinas, comprovando o resultado obtido com o alinhamento das seq??ncias prim?rias; o motivo R&R, apesar de n?o ter semelhan?a estrutural nas vicilinas, provavelmente tem uma participa??o na atividade de intera??o destas com GlcNac; enquanto que o motivo CD participa diretamente na intera??o das vicilinas com GlcNac. Estes resultados in silico mostram que o n?mero de amino?cidos, os tipos e a quantidade de liga??es feitas pelo motivo CD com GlcNac parecem estar diretamente associados ao poder delet?rio que essas vicilinas possuem para larvas de C. maculatus. Isso pode constutuir um passo inicial na elucida??o de como as vicilinas interagem com quitina in vivo e exercem seu poder t?xico para insetos que possuem membrana peritr?fica
| Identifer | oai:union.ndltd.org:IBICT/oai:repositorio.ufrn.br:123456789/12545 |
| Date | 06 February 2009 |
| Creators | Aquino, Rodrigo Oliveira de |
| Contributors | CPF:29706106391, http://lattes.cnpq.br/7890362793618911, Santos, Elizeu Antunes dos, CPF:41305655400, http://buscatextual.cnpq.br/buscatextual/visualizacv.do?id=K4782221T9&dataRevisao=null, Franco, Oct?vio Luiz, CPF:75523400378, http://lattes.cnpq.br/8598274096498065, Sales, Maur?cio Pereira de |
| Publisher | Universidade Federal do Rio Grande do Norte, Programa de P?s-Gradua??o em Bioqu?mica, UFRN, BR, Bioqu?mica; Biologia Molecular |
| Source Sets | IBICT Brazilian ETDs |
| Language | Portuguese |
| Detected Language | English |
| Type | info:eu-repo/semantics/publishedVersion, info:eu-repo/semantics/masterThesis |
| Format | application/pdf |
| Source | reponame:Repositório Institucional da UFRN, instname:Universidade Federal do Rio Grande do Norte, instacron:UFRN |
| Rights | info:eu-repo/semantics/openAccess |
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