Chemical effect of hydrodynamic cavitation: Simulation and experimental comparison

The chemical effect of hydrodynamic cavitation (HC) in a Venturi reactor from both the theoretical and the experimental point of view is dealt. A mathematical model is presented to simulate the global production of hydroxyl radicals; it is based on a set of ordinary differential equations that account for the hydrodynamics, mass diffusion, heat exchange, and chemical reactions inside the bubbles. Experimentally, the degradation of p‐nitrophenol (initial concentration 0.15 g dm^?3) has been conducted in a lab scale Venturi reactor at inlet pressure ranging from 0.2 to 0.6 MPa and has been used to estimate the hydroxyl radical production. The optimum configuration, suggested by numerical simulations, has been experimentally confirmed. Thanks to the empirical validation, this novel modeling approach can be considered as a theoretical tool to identify the best configuration of HC operating parameters. © 2014 American Institute of Chemical Engineers AIChE J, 60: 2566–2572, 2014     

Silicon analogues of the retinoid agonists TTNPB and 3-methyl-TTNPB, disila-TTNPB and disila-3-methyl-TTNPB: chemistry and biology

Twofold sila-substitution (C/Si exchange) in the saturated ring of the tetrahydronaphthalene skeleton of the retinoid agonists TTNPB (1 a) and 3-methyl-TTNPB (2 a) leads to disila-TTNPB (1 b) and disila-3-methyl-TTNPB (2 b), respectively. The silicon compounds 1 b and 2 b were synthesized in multiple steps, and their identities were established by elemental analyses, multinuclear NMR experiments, and single-crystal X-ray diffraction studies. Like TTNPB (1 a) and 3-methyl-TTNPB (2 a), the analogous silicon-based arotinoids 1 b and 2 b are strong pan-RAR agonists and display the same strong differentiation and apoptosis-inducing activity in NB4 promyelocytic leukemia cells as the parent carbon compounds. These results are in keeping with the nearly isomorphous structures of 1 a and 1 b bound to the complex of the RARbeta ligand-binding domain with the nuclear receptor (NR) box 2 peptide of the SRC-1 coactivator. The contacts within the ligand-binding pocket are identical except for helix H11, for which two turns are shifted in the disila-TTNPB (1 b) complex. This study represents the first comprehensive structure-function analysis of a carbon/silicon switch in a signaling molecule and demonstrates that silicon analogues can have the same biological functionalities and conserved structures as their parent carbon compounds, and it illustrates at the same time that silicon analogues of biologically active compounds have the potential to induce alternative allosteric effects, as in the case of helix H11, which might allow for novel options in drug design.