Structural analysis of the interaction between Jaburetox, an intrinsically disordered protein, and membrane models

摘要: Abstract Jack bean urease is entomotoxic to insects with cathepsin-like digestive enzymes, and its toxicity mainly caused by a polypeptide called Jaburetox (Jbtx), released cathepsin-dependent hydrolysis of the enzyme. Jbtx intrinsically disordered in aqueous solution, as shown CD NMR. able alter permeability membranes, hinting role Jbtx-membrane interaction basis for toxicity. The present study addresses structural aspects this investigating behaviour when contact membrane models, using nuclear magnetic resonance circular dichroism spectroscopies absence or presence micelles, large unilamellar vesicles, bicelles. Fluorescence microscopy was also used detect protein-insect interaction. Significant differences were observed depending on type model used. negatively charged SDS micelles increases secondary tertiary structure content polypeptide, while, case vesicles bicelles, conformational changes at terminal regions, no significant acquisition motifs. These results interpreted suggesting that Jbtx-lipids anchors cellular through portions that, following interaction, undergoes achieve more ordered could facilitate membrane-bound proteins. Consistently hypothesis, these models decreases ability bind membranes insect nerve cord. collected evidence from studies implies biological activity due protein-phospholipid interactions.