Characterization of nanospherical silicate particles by nitrogen adsorption and SEM imaging: NS (black), NS-G (blue), NS-T (green), and NS-B (red).

<p><b>A.</b> Nitrogen adsorption/desorption isotherms. <b>B.</b> Pore size distributions. <b>C.</b> SEM image. <b>D.</b> Particle diameter distribution determined from SEM images.</p

Recovery of RNA adsorbed onto sorbents following storage at 4°C.

<p>Data is presented as the ratio of the RNA recovered on a given day to that recovered for the same sorbent on day one of the experiment. Recovery of RNA from NS (black), NS-G (blue) NS-T (green), and NS-B (red) sorbents. An RNA control in water under identical storage conditions was also monitored over this time period (gray).</p

Schematic representations of synthesis and functionalization of nanospherical silicate particles.

<p>Schematic representations of synthesis and functionalization of nanospherical silicate particles.</p

Environmental Decontamination of a Chemical Warfare Simulant Utilizing a Membrane Vesicle-Encapsulated Phosphotriesterase

While technologies for the remediation of chemical contaminants continue to emerge, growing interest in green technologies has led researchers to explore natural catalytic mechanisms derived from microbial species. One such method, enzymatic degradation, offers an alternative to harsh chemical catalysts and resins. Recombinant enzymes, however, are often too labile or show limited activity when challenged with nonideal environmental conditions that may vary in salinity, pH, or other physical properties. Here, we demonstrate how phosphotriesterase encapsulated in a bacterial outer membrane vesicle can be used to degrade the organophosphate chemical warfare agent (CWA) simulant paraoxon in environmental water samples. We also carried out remediation assays on solid surfaces, including glass, painted metal, and fabric, that were selected as representative materials, which could potentially be contaminated with a CWA

Proteolytic Activity at Quantum Dot-Conjugates: Kinetic Analysis Reveals Enhanced Enzyme Activity and Localized Interfacial “Hopping”

Recent studies show that polyvalent, ligand-modified nanoparticles provide significantly enhanced binding characteristics compared to isolated ligands. Here, we assess the ability of substrate-modified nanoparticles to provide enhanced enzymatic activity. Energy transfer assays allowed quantitative, real-time measurement of proteolytic digestion at polyvalent quantum dot-peptide conjugates. Enzymatic progress curves were analyzed using an integrated Michaelis–Menten (MM) formalism, revealing mechanistic details, including deviations from classic MM-behavior. A “hopping” mode of proteolysis at the nanoparticle was identified, confirming enhanced activity