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LyeTx I, a potent antimicrobial peptide from the venom of the spider Lycosa erythrognatha.
Santos, D M; Verly, R M; Piló-Veloso, D; de Maria, M; de Carvalho, M A R; Cisalpino, P S; Soares, B M; Diniz, C G; Farias, L M; Moreira, D F F; Frézard, F; Bemquerer, M P; Pimenta, A M C; de Lima, M E.
Afiliação
  • Santos DM; Lab. Venenos e Toxinas Animais, Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, 31270-901, Belo Horizonte, Minas Gerais, Brazil.
Amino Acids ; 39(1): 135-44, 2010 Jun.
Article em En | MEDLINE | ID: mdl-19946788
LyeTx I, an antimicrobial peptide isolated from the venom of Lycosa erythrognatha, known as wolf spider, has been synthesised and its structural profile studied by using the CD and NMR techniques. LyeTx I has shown to be active against bacteria (Escherichia coli and Staphylococcus aureus) and fungi (Candida krusei and Cryptococcus neoformans) and able to alter the permeabilisation of L: -alpha-phosphatidylcholine-liposomes (POPC) in a dose-dependent manner. In POPC containing cholesterol or ergosterol, permeabilisation has either decreased about five times or remained unchanged, respectively. These results, along with the observed low haemolytic activity, indicated that antimicrobial membranes, rather than vertebrate membranes seem to be the preferential targets. However, the complexity of biological membranes compared to liposomes must be taken in account. Besides, other membrane components, such as proteins and even specific lipids, cannot be discarded to be important to the preferential action of the LyeTx I to the tested microorganisms. The secondary structure of LyeTx I shows a small random-coil region at the N-terminus followed by an alpha-helix that reached the amidated C-terminus, which might favour the peptide-membrane interaction. The high activity against bacteria together with the moderate activity against fungi and the low haemolytic activity have indicated LyeTx I as a good prototype for developing new antibiotic peptides.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Venenos de Aranha / Peptídeos Catiônicos Antimicrobianos / Antibacterianos / Antifúngicos Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Revista: Amino Acids Assunto da revista: BIOQUIMICA Ano de publicação: 2010 Tipo de documento: Article País de afiliação: Brasil País de publicação: Áustria

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Venenos de Aranha / Peptídeos Catiônicos Antimicrobianos / Antibacterianos / Antifúngicos Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Revista: Amino Acids Assunto da revista: BIOQUIMICA Ano de publicação: 2010 Tipo de documento: Article País de afiliação: Brasil País de publicação: Áustria