title: LyeTx I, a potent antimicrobial peptide from the venom of the spider Lycosa erythrognatha.
abstract: 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.
authors: 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.
authors: D M
authors: DM
authors: Santos
authors: R M
authors: RM
authors: Verly
authors: D
authors: D
authors: Piló-Veloso
authors: M
authors: M
authors: de Maria
authors: M A R
authors: MA
authors: de Carvalho
authors: P S
authors: PS
authors: Cisalpino
authors: B M
authors: BM
authors: Soares
authors: C G
authors: CG
authors: Diniz
authors: L M
authors: LM
authors: Farias
authors: D F F
authors: DF
authors: Moreira
authors: F
authors: F
authors: Frézard
authors: M P
authors: MP
authors: Bemquerer
authors: A M C
authors: AM
authors: Pimenta
authors: M E
authors: ME
authors: de Lima
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D000935:Antifungal Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D002175:Candida / Q000187:drug effects; D003455:Cryptococcus neoformans / Q000187:drug effects; D004305:Dose-Response Relationship, Drug; D004926:Escherichia coli / Q000187:drug effects; D008826:Microbial Sensitivity Tests; D008958:Models, Molecular; D010713:Phosphatidylcholines / Q000037:antagonists & inhibitors; D017433:Protein Structure, Secondary; D013111:Spider Venoms / Q000737:chemistry*; D013112:Spiders; D013211:Staphylococcus aureus / Q000187:drug effects
chemical_list: D000900:Anti-Bacterial Agents; D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; C552026:LyeTx I protein, Lycosa erythrognatha; D010713:Phosphatidylcholines; D013111:Spider Venoms; C028694:1-palmitoyl-2-oleoylphosphatidylcholine