Reduced pH induces an inactive non-native conformation of the monomeric bothropstoxin-I (Lys49-PLA<sub>2</sub>)期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

Reduced pH induces an inactive non-native conformation of the monomeric bothropstoxin-I (Lys49-PLA₂)

Authors:	Arthur H.C. de Oliveira Tatiana L. Ferreira

Affiliation:	^a Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Avenida Bandeirantes 3900, CEP 14040-901, Ribeirão Preto, SP, Brazil ^b Verdartis Desenvolvimento Biotecnológico Ltda ME, Campus USP, Ribeirão Preto, SP, Brazil

Abstract:	Bothropstoxin-I (BthTx-I), a Lys49-PLA₂ from Bothrops jararacussu venom, permeabilizes membranes by a non-hydrolytic Ca²⁺-independent mechanism. The BthTx-I showed activity against liposomes including 10% and 50% negatively charged lipids at pH 7.0, but not at pH 5.0. Nevertheless, ultracentrifugation and FRET demonstrated that at pH 5.0 the BthTx-I is bound to 50% negatively charged membranes. ANS binding identified a non-native monomeric conformation at pH 5.0, suggesting that tertiary structure alterations result in activity loss of the BthTx-I at low pH.

Keywords:	Phospholipase A₂ Membrane permeabilization Molten globule
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