Quantitative model for predicting the electroosmotic flow in dual-pole nanochannels.

Developing and assessing nanofluidic systems is time-consuming and costly owing to the method's novelty; hence, modeling is essential to determine the optimal areas for implementation and to grasp its workings. In this work, we examined the influence of dual-pole surface and nanopore configuration on ion transfer simultaneously. To achieve this, the two trumpet and cigarette configuration were coated with a dual-pole soft surface so that the negative charge could be positioned in the nanopore's small aperture. Subsequently, the Poisson-Nernst-Planck and Navier-Stokes equations were simultaneously solved under steady-state circumstances using varied values physicochemical properties for the soft surface and electrolyte. The pore's selectivity was S Trumpet > S Cigarette ${S}_{{\rm{Trumpet}}} > {S}_{{\rm{Cigarette}}}$ , and the rectification factor, on the other hand, was R f Cigarette < R f Trumpet ${R}_{{f}_{{\rm{Cigarette}}}} < {R}_{{f}_{{\rm{Trumpet}}}}$ , when the overall concentration was very low. When the ion partitioning effect is taken into account, we clearly show that the rectifying variables for the cigarette configuration and the trumpet configuration can reach values of 45 and 49.2, when the charge density and mass concentration were 100 mol/m3 and 1 mM, respectively. By using dual-pole surfaces, the controllability of nanopores' rectifying behavior may be modified to produce superior separation performance.

Rational Design, Synthesis, in Vitro, and in Silico Studies of Chlorophenylquinazolin-4(3H)-One Containing Different Aryl Acetohydrazides as Tyrosinase Inhibitors.

Tyrosinase plays a pivotal role in the hyperpigmentation and enzymatic browning of fruit and vegetable. Therefore, tyrosinase inhibitors can be of interest in industries as depigmentation compounds as well as anti-browning agents. In the present study, a series of chlorophenylquinazolin-4(3H)-one derivative were rationally designed and synthesized. The formation of target compounds was confirmed by spectral characterization techniques such as IR, 1 H-NMR, 13 C-NMR, and elemental analysis. Among the synthesized derivatives, compound 8l was proved to be the most potent inhibitor with an IC50 value of 25.48±1.19 µM. Furthermore, the results of the molecular docking study showed that this compound fitted well in the active site of tyrosinase with the binding score of -10.72.