Publications by authors named "Nathalie Sorde"
Recently, synthetic multifunctional pores have been identified as "universal" detectors of chemical reactions. In this report, we show that with the assistance of enzymes as variable co-sensors, synthetic multifunctional pores can serve as similar universal sensors of variable components in mixed analytes. Sugar sensing in soft drinks is used to exemplify this new concept.
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- The study compares pores created by p-octiphenyl beta-barrels with LWV triads to traditional rigid-rod beta-barrels, highlighting the multifunctional abilities of the tetrameric pores.
- The findings indicate that the preference for membrane interaction is influenced by the bilayer's affinity to W, which is greater than to V, suggesting a preference for barrel-stave over toroidal pore structures.
- The research also discusses how the stability of these pore formations is affected by monomer concentration, revealing a trend where lower beta-propensity for W leads to less stable conditions compared to V.
This report delineates scope and limitation of the selectivity of synthetic multifunctional pores as enzyme sensors using glycolytic enzymes as example (G. Das, P. Talukdar, and S.
View Article and Find Full Text PDFEnzyme screening with synthetic multifunctional pores: focus on biopolymers.
Proc Natl Acad Sci U S A
October 2003
This report demonstrates that a single set of identical synthetic multifunctional pores can detect the activity of many different enzymes. Enzymes catalyzing either synthesis or degradation of DNA (exonuclease III or polymerase I), RNA (RNase A), polysaccharides (heparinase I, hyaluronidase, and galactosyltransferase), and proteins (papain, ficin, elastase, subtilisin, and pronase) are selected to exemplify this key characteristic of synthetic multifunctional pore sensors. Because anionic, cationic, and neutral substrates can gain access to the interior of complementarily functionalized pores, such pores can be the basis for very user-friendly screening of a broad range of enzymes.
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- The study investigates the properties of beta-barrel ion channels featuring internal aspartates and arginine-histidine pairs through bilayer conductance experiments.
- The aspartate-containing channels exhibit cation selectivity but are unstable, with magnesium cations improving stability while diminishing selectivity.
- In contrast, arginine-histidine channels are stable, cation-selective, and exhibit unique behaviors with changes in pH and the presence of anionic molecules, highlighting the potential of these internal structures to enhance channel functionality.
Catalytic activity of a synthetic multifunctional pore is studied in large unilamellar vesicles under conditions where substrate and synthetic catalytic pore (SCP) approach the membrane either from the same side (cis catalysis) or from opposite sides (trans catalysis). A synthetic supramolecular rigid-rod beta-barrel with excellent ion channel characteristics is identified as SCP using 8-acetoxypyrene-1,3,6-trisulfonate (AcPTS) as model substrate. The key finding is that application of supportive membrane potentials increases the initial velocity of AcPTS esterolysis (v0).
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