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In this study, a series of novel bis-sulfone compounds (2a-2j) were synthesized by oxidation of the bis-sulfides under mild reaction conditions. The bis-sulfone derivatives were characterized by 1 H-NMR, 13 C-NMR, Fourier-transform infrared spectroscopy, and elemental analysis techniques. Nuclear Overhauser effect experiments were performed to determine the orientation of the sulfonyl groups in bis-sulfone derivatives. Here, we report the synthesis and testing of novel bis-sulfone compound-based hybrid scaffold of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitors for the development of novel molecules toward the therapy of Alzheimer's disease. The novel synthesized bis-sulfone compounds demonstrated K i values between 11.4 ± 3.4 and 70.7 ± 23.2 nM on human carbonic anhydrase I isozyme (hCA I), 28.7 ± 6.6 to 77.6 ± 5.6 nM on human carbonic anhydrase II isozyme (hCA II), 18.7 ± 2.61 to 95.4 ± 25.52 nM on AChE, and 9.5 ± 2.1 to 95.5 ± 1.2 nM on BChE enzymes. The results showed that novel bissulfone derivatives can have promising drug potential for glaucoma, leukemia, epilepsy, and Alzheimer's disease, which are associated with the high enzymatic activity of hCA I, hCA II, AChE, and BChE enzymes. K E Y W O R D S acetylcholinesterase, bis-sulfide, butyrylcholinesterase, bis-sulfone, carbonic anhydrase

Two bis-chalcone derivatives, (2E,6E)-2,6-bis[(thiophen-2-yl)methylene]cyclohexanone (C1) and (2E,6E)-2,6-bis[(furan-2yl)methylene]cyclohexanone (C2)-based electrochromic (EC) nanofibers were produced in the presence of poly(methyl methacrylate) (PMMA) as supporting polymer using the electrospinning technique. The scanning electron microscopy (SEM) and energy dispersive X-ray spectroscopy were used to examine morphology and chemical compositions of nanofibers before and after stability test. SEM images of the obtained smooth and bead-free nanofibers before the stability test showed that both bis-chalcone derivatives were homogeneously dispersed on the surface of the electrospun nanofibers. Nanofibers of bis-chalcone derivatives were characterized with Fourier-transform infrared spectroscopy. The electrochemical and EC properties of these bis-chalcone derivatives were investigated. The C1-PMMA nanofiber-based electrochromic device (ECD) showed higher DT max (41.47%) than that of the C2-PMMA nanofiberbased ECD (4.67%) during coloration/bleaching at 715 nm. The switching times for coloration and bleaching of C1-PMMA nanofiber-based ECD were found to be 4.42 and 1.12 s, respectively, and the coloration efficiency was 136.18 cm 2 /C. Repeated cyclic voltammograms and 1000 cycles of chronoamperometric measurements of the bis-chalcone derivatives indicated that ECDs have long-term redox stability.

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Aldose reductase (AR, ALR2; EC 1.1.1.21), an enzyme that converts glucose to fructose on the polyol pathway, is an important member of the Aldo-keto reductase superfamily. ALR2 is part of the rate-limiting step, which is associated with diabetic complications in this process, and plays a role in regulating reactive oxygen species induced by growth factors and cytokines. Despite the fact that sulfides and sulfones have been discovered to have a variety of other biological functions, in the current study, we assessed the ALR2 inhibitory potential of the derivatives of bis-sulfide (5 a-i) and bis-sulfone (6 a-i) in order to further our interest in designing and discovering powerful ALR2 inhibitors. The results of the biological investigations showed that all of the derivatives exhibit activity against ALR2, with K I values ranging from 0.53 � 0.03 to 4.20 � 0.06 μM.Among these agents, 2,6-bis((4-chlorophenyl)(phenylthio)methyl)cyclohexan-1-one (5 h), 2,6bis((3-nitrophenyl)(phenylthio)methyl)cyclohexan-1-one (5 c), and 2,6-bis((3-chlorophenyl)(phenylthio)methyl)cyclohexan-1one (5 g) exhibited prominent inhibitory activity with K I constants of 0.53 � 0.03 μM, 0.65 � 0.04 μM, and 0.71 � 0.05 μM, respectively, against ALR2 and were found to be more potent than epalrestat (K I = 0.79 � 0.01 μM) is currently, the only ALR2 inhibitor (ALR2I) utilized in treatment. Additionally, in silico molecular docking experiments were carried out to explain how these bis-sulfides (5 a-i) and bis-sulfones (6 a-i) interacted with the target enzyme ALR2's binding site. According to the ADME-Tox study, these compounds are predicted to be ALR2Is with appropriate drug-like characteristics. The study's findings on sulfides and sulfones could be exploited to create innovative therapeutics that prevent diabetes complications.

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