Discovery of Novel Pyrazole Acyl Thiourea Skeleton Analogue as Potential Herbicide Candidates.

To discover novel transketolase (TKL, EC 2.2.1.1) inhibitors with potential herbicidal applications, a series of pyrazole acyl thiourea derivatives were designed based on a previously obtained pyrazolamide acyl lead compound, employing a scaffold hopping strategy. The compounds were synthesized, their structures were characterized, and they were evaluated for herbicidal activities. The results indicate that 7a exhibited exceptional herbicidal activity against Digitaria sanguinalis and Amaranthus retroflexus at a dosage of 90 g ai/ha, using the foliar spray method in a greenhouse. This performance is comparable to that of commercial products, such as nicosulfuron and mesotrione. Moreover, 7a showed moderate growth inhibitory activity against the young root and stem of A. retroflexus at 200 mg/L in the small cup method, similar to that of nicosulfuron and mesotrione. Subsequent mode-of-action verification experiments revealed that 7a and 7e inhibited Setaria viridis TKL (SvTKL) enzyme activity, with IC50 values of 0.740 and 0.474 mg/L, respectively. Furthermore, they exhibited inhibitory effects on the Brassica napus acetohydroxyacid synthase enzyme activity. Molecular docking predicted potential interactions between these (7a and 7e) and SvTKL. A greenhouse experiment demonstrated that 7a exhibited favorable crop safety at 150 g ai/ha. Therefore, 7a is a promising herbicidal candidate that is worthy of further development.

Insight into intermolecular binding mechanism of apatinib mesylate and human alpha-1-acid glycoprotein: combined multi-spectroscopic approaches with in silico.

Apatinib mesylate (APM), an oral tyrosine kinase inhibitor, has a good anti-tumor activity in the treatment of various cancers, particularly in advanced non-small cell lung cancer. In this study, the intermolecular binding mechanism between APM and human alpha-1-acid glycoprotein (HAG) was investigated by combining multi-spectroscopic approaches with in silico techniques. The findings revealed that APM gave rise to the fluorescence quenching of HAG by forming a ground-state complex between APM and HAG with a stoichiometric ratio of 1:1, and APM has a moderate affinity for HAG as the binding constant of APM and HAG of approximately 105 M-1, which was larger than the APM-HAG complex. The findings from thermodynamic parameter analysis indicated that the dominant driving forces for the formation of the APM-HAG complex were van der Waals forces, hydrogen bonding and hydrophobic interactions, which were also verified with site-probe studies and molecular docking. The findings from in silico study indicated that APM inserted into the opening of the hydrophobic cavity of HAG, leads to a slight conformational change in the HAG, which was verified by circular dichroism (CD) measurements, that was, the beta sheet level of HAG decreased. Additionally, the results of synchronous and 3D fluorescence spectroscopies confirmed the decline in hydrophobicity of the microenvironment around Trp and Tyr residues. Moreover, some common metal ions such as Cu2+, Mg2+, Fe3+, Ca2+, and Zn2+ could cause the alteration in the binding constant of APM with HAG, leading to the change in the efficacy of APM. It will be expected that these study findings are to provide useful information for further understanding pharmacokinetic and structural modifications of APM.Communicated by Ramaswamy H. Sarma.

Investigation on the binding behavior of human α1-acid glycoprotein with Janus Kinase inhibitor baricitinib: Multi-spectroscopic and molecular simulation methodologies.

Baricitinib is a Janus Kinase (JAK) inhibitor that is primarily used to treat moderately to severely active rheumatoid arthritis in adults and has recently been reported for the treatment of patients with severe COVID-19. This paper describes the investigation of the binding behavior of baricitinib to human α1-acid glycoprotein (HAG) employing a variety of spectroscopic techniques, molecular docking and dynamics simulations. Baricitinib can quench the fluorescence from amino acids in HAG through a mix of dynamic and static quenching, according to steady-state fluorescence and UV spectra observations, but it is mainly static quenching at low concentration. The binding constant (Kb) of baricitinib to HAG at 298 K was at the level of 104 M-1, indicating a moderate affinity of baricitinib to HAG. Hydrogen bonding and hydrophobic interactions conducted the main effect, according to thermodynamic characteristics, competition studies between ANS and sucrose, and molecular dynamics simulations. For the change in HAG conformation, the results of multiple spectra showed that baricitinib was able to alter the secondary structure of HAG as well as increase the polarity of the microenvironment around the Trp amino acid. Furthermore, the binding behavior of baricitinib to HAG was investigated by molecular docking and molecular dynamics simulations, which validated experimental results. Also explored is the influence of K+, Co2+, Ni2+, Ca2+, Fe3+, Zn2+, Mg2+ and Cu2+plasma on binding affinity.

Elucidation of the interaction mechanism of olmutinib with human α-1 acid glycoprotein: insights from spectroscopic and molecular modeling studies.

Olmutinib, the third-generation tyrosine kinase inhibitor, is applied in treating non-small cell lung cancer (NSCLC). The aim of this study is to elucidate the interaction mechanism of olmutinib with human α-1 acid glycoprotein (HAG), an important carrier protein, by mean of multi-spectroscopic and molecular simulation techniques. Fluorescence spectral results confirmed that the fluorescence of this carrier protein can be quenched by olmutinib in the static quenching mode, and this anticancer drug possesses a moderate binding affinity on HAG. The evidence from thermodynamic analysis, replacement interaction with ANS and sucrose, and computational simulation results showed that hydrogen bonding, hydrophobic interactions, and van der Waals forces involved the olmutinib-HAG complexation process. The results from UV-vis, 3D fluorescence and synchronous fluorescence spectroscopy proved that binding anticancer drug olmutinib caused the alteration in the microenvironment around Trp residues. And, circular dichroism spectral results provided the support for the conformational alterations in the carrier protein. The data also proved that olmutinib preferably bound to the hydrophobic cavity of HAG and the binding distance between the two was 2.21 nm. In addition, it can be found that the presence of some metal ions such as Zn2+, Ca2+, Ni2+ and Cu2+ would exert a certain extent effect on the olmutinib-HAG complexation process.Communicated by Ramaswamy H. Sarma.

Synthesis of Indoles via Domino Reactions of 2-Methoxytoluene and Nitriles.

2-Arylindoles are privileged structures widely present in biologically active molecules. New sustainable synthetic routes toward their synthesis are, therefore, in high demand. Herein, a mixed base-promoted benzylic C-H deprotonation of commercially available ortho-anisoles, addition of the resulting anion to benzonitriles, and SNAr to displace the methoxy group provide indoles. A diverse array of 2-arylindoles is prepared with good yields (>30 examples, yields up to 99%) without added transition metal catalysts.

Comprehending binding features between ibrutinib and Human Alpha-1 acid glycoprotein: Combined experimental approaches and theoretical simulations.

Human alpha-1 acidic glycoprotein (HAG) is one of the proteins widely present in the blood, and the level of HAG in patients with cancer and inflammation is significantly increased. As one of transport proteins in the blood, the ability of HAG to bind with a drug, especially alkaline drugs, affects significantly the drug content at the target site, which in turn affects the efficacy of the drug. In this study, the interaction mechanism between HAG and the first generation Bruton's tyrosine kinase (BTK) inhibitor namely ibrutinib was explored by a combination of multi-spectroscopic techniques and theoretical calculations. The findings revealed that the quenching and binding constants of the HAG-ibrutinib system both reduced as the temperature rose, demonstrating that ibrutinib quenched the intrinsic fluorescence of HAG in a static manner. It was confirmed that HAG and ibrutinib formed a 1:1 complex with moderate affinity due to the binding constant of around 105 M-1 and accompanied by Förster resonance energy transfer. It was verified by thermodynamic parameter analysis and competition assays as well as molecular simulation that the existence of hydrogen bonds, van der Waals forces, and hydrophobic forces in the complexation of HAG and ibrutinib.The findings from theoretical calculations including molecular docking and theoretical calculation simulation confirmed that ibrutinib bound to the barrel hydrophobic pocket of HAG with a binding energy of -41.9 kJ∙mol-1, and the the binding constant of around 105 M-1 and the contribution of each residue in the complexation of ibrutinib and HAG. Additionally, it can be confirmed that metal ions affected the binding interaction of ibrutinib with HAG, among them, some promoted binding while others inhibited it.

Design, Synthesis, and Evaluation of Novel 4-Chloropyrazole-Based Pyridines as Potent Fungicide Candidates.

A rational molecular design approach was developed in our laboratory to guide the discovery of novel sterol biosynthesis inhibitors. Based on the application of bioactivities of heterocyclic rings and molecular docking targeting the sterol biosynthesis 14α-demethylase, a series of 4-chloropyrazole-based pyridine derivatives were rationally designed, synthesized, and characterized and their fungicidal activities were also evaluated. Bioassay results showed that 7e, 7f, and 7m exhibited commendable, diverse antifungal actions that are comparable to those of the positive controls imazalil and triadimefon. The active compounds' mode of action was further studied by microscopy observations, Q-PCR, and enzyme inhibition assay and discovered that target compounds affect fungal sterol biosynthesis via disturbing RcCYP51 enzyme system. These findings support that their fungicidal mode of action still targets the cytochrome P450-dependent 14α-demethylase as the molecular design did at first. The above results strongly suggest that our rational molecular design protocol is not only practical but also efficient.

2-Arylindoles: Concise Syntheses and a Privileged Scaffold for Fungicide Discovery.

Indole is a popular and functional scaffold existing widely in the fields of medicine, pesticides, spices, food and feed additives, dyes, and many others. Among indoles, 2-arylindole represents a particular and interesting subset but has attracted less attention for drug discovery. In this study, we report a general, practical one-pot assembly of a variety of 2-arylindole derivatives. To develop novel fungicide scaffolds, their fungicide activity was also evaluated. The bioassay results showed that many of the synthesized 2-arylindoles exhibited considerable fungicidal activities especially toward Rhizoctonia cerealis, and several demonstrated an inhibition rate of more than 90%. Notably, 4-fluoro-2-phenyl-1H-indole 6e was obtained with a broad spectrum of fungicidal activities, which showed excellent growth inhibition activities against R. cerealis, Rhizoctonia solani, Botrytis cinerea, Magnaporthe oryza, and Sclerotinia sclerotiorum with EC50 values of 2.31, 4.98, 6.78, 10.57, and 17.80 µg/mL, respectively. Preliminary fungicidal mode of action of 6e showed a significant inhibition effect on mycelial growth and spore germination. These results indicated that 2-arylindoles as privileged scaffolds exhibited potential fungicidal activities that deserve further study.

Discovery of Novel Pyrazole Amides as Potent Fungicide Candidates and Evaluation of Their Mode of Action.

A rational molecule design strategy based on scaffold hopping was applied to discover novel leads, and then a series of novel pyrazole amide derivatives were designed, synthesized, characterized, and evaluated for their antifungal activities. Bioassay results indicated that some target compounds such as S3, S12, and S26 showed good in vivo antifungal activities; among them, S26 exhibited commendable in vivo protective activity with an 89% inhibition rate against Botrytis cinerea on cucumber at 100 µg/mL that is comparable to positive controls boscalid, isopyrazam, and fluxapyroxad. Microscopy observations suggested that S26 affects the normal fungal growth. Fluorescence quenching analysis and SDH (succinate dehydrogenase) enzymatic inhibition studies validated that S26 may not be an SDH inhibitor. Based on induction of plant defense responses testing, S26 enhanced the accumulation of RBOH, WRKY6, WRKY30, PR1, and PAL defense-related genes expression and the defense-associated enzyme phenylalanine ammonia lyase (PAL) expression on cucumber. These findings support that S26 not only displayed direct fungicidal activity but also exhibited plant innate immunity stimulation activity, and it could be used as a promising plant defense-related fungicide candidate.

Exploring the inclusion interaction of estradiol with ß-CD and HP-ß-CD with the help of molecular dynamics simulation as well as multi-spectroscopic approaches.

The inclusion behaviors of estradiol with ß-CD and HP-ß-CD were characterized using molecular dynamics simulation combined with multi-spectroscopic approaches. The findings revealed that estradiol enclosed into the cavity of ß-CD and HP-ß-CD and produced the estradiol-ß-CD and estradiol-HP-ß-CD complexes with the stoichiometry of 1:1. The association constants of the estradiol-ß-CD and estradiol-HP-ß-CD complexes were 3.14 × 104 and 3.22 × 104 M-1 at 298 K, respectively, which declined with rising temperature. The analysis results of thermodynamic parameters confirmed that the dominate interaction forces were the hydrophobic and hydrogen-bonding interactions for stabilizing the estradiol-ß-CD complex, and were the hydrogen bonding interaction and van der Waals forces for stabilizing the estradiol-HP-ß-CD complex. Moreover, it was confirmed from the results of molecular modeling that estradiol inserted into the hydrophobic cavity of ß-CD and HP-ß-CD and form a stable estradiol-CD complexes. And, it is also observed that the phenyl moiety in estradiol is almost parallel to the central axis of ß-CD and HP-ß-CD, and the phenyl moiety was located on wider rim of ß-CD and HP-ß-CD.

Investigation of binding characteristics of ritonavir with calf thymus DNA with the help of spectroscopic techniques and molecular simulation.

The binding behavior of ritonavir (RTV), a HIV/AIDS protease inhibitor, with ct-DNA was characterized through multiple testing technologies and theoretical calculation. The findings revealed that the RTV-DNA complex was formed through the noncovalent interaction mainly including conventional hydrogen bonds and carbon hydrogen bonds as well as hydrophobic interactions (pi-alkyl interactions). The stoichiometry and binding constant of the RTV-DNA complex were 1:1 and 1.87 × 103 M-1 at 298 K, respectively, indicating that RTV has moderate affinity with ct-DNA. The findings confirmed that RTV binds to the minor groove of DNA. The outcomes of CD experiments showed that the binding with RTV changed the conformation of DNA slightly. However, the conformation of RTV had obvious changes after binding to DNA, meaning that the flexibility of RTV molecule played an important role in stabilizing the RTV-DNA complex. Meanwhile, the results of DFT calculation revealed that the RTV and DNA interaction caused the changes in the frontier molecular orbitals, dipole moment and atomic charge distribution of RTV, altering the chemical properties of RTV when it bound to DNA. Communicated by Ramaswamy H. Sarma.

Enantioseparation of mandelic acid and substituted derivatives by high-performance liquid chromatography with hydroxypropyl-ß-cyclodextrin as chiral mobile additive and evaluation of inclusion complexes by molecular dynamics.

The enantioseparation and resolution mechanism of mandelic acid (MA), 4-methoxymandelic acid (MMA), and 4-propoxymandelic acid (PMA) were investigated by reversed-phase high-performance liquid chromatography (HPLC) with 2-hydroxypropyl-ß-cyclodextrin (HP-ß-CD) as a chiral mobile-phase additive and molecular dynamics simulation. The suitable chromatographic conditions for the enantioseparation of MA, MMA, and PMA were obtained. Under the selected chromatographic conditions, these enantiomers could achieve baseline separation. The results of thermodynamic parameter analysis revealed that the main driven forces for the enantioseparation of MA, MMA, and PMA could be van der Waals forces and hydrogen-bonding interactions and the chromatographic retention of these chiral compounds was an enthalpy-driven process. The results of the molecular simulation revealed that their chiral resolution mechanism on HP-ß-CD was responsible for the formation of inclusion complexes of enantiomers with HP-ß-CD with different conformations and binding energies. And the binding energy of HP-ß-CD with (S)-isomer was larger than that with (R)-isomer, which is consistent with the experimental results of the first elution of (S)-isomer. Additionally, it is also confirmed that the interaction energies included the van der Waals energy (∆Evdw ), electrostatic energy (∆Eelec ), polar solvation energy, and SASA energy (∆Esasa ), and the separation factor (α) was closely connected with the disparity in the binding energies of optical isomers and HP-ß-CD complexes. Meanwhile, from molecular dynamics simulation, it can be found that the ∆(∆Ebinding ), (∆(∆Ebinding ) = ∆Ebinding,R - ∆Ebinding,S ) value was in order of MA-HP-ß-CD complex > MMA-HP-ß-CD complex > PMA-HP-ß-CD complex, which was consistent with the order of Δ(ΔG) values obtained from van't Hoff plot. This indicated that the molecular dynamics simulation has predictive function for chiral resolution.

One-Pot Synthesis of N-H-Free Pyrroles from Aldehydes and Alkynes.

The first base-mediated intermolecular cyclization of arylaldehydes and terminal arylacetylenes for the synthesis of a wide range of pyrroles in a single step has been described. The developed methodology used commercially available starting materials and tolerated a broad range of functional groups affording 2,3,5-triaryl-substituted-1H-pyrroles with good yields (up to 92% yield) under mild conditions. The possible mechanism was also discussed.

Evaluation of the interaction of novel tyrosine kinase inhibitor apatinib mesylate with bovine serum albumin using spectroscopies and theoretical calculation approaches.

Apatinib mesylate (APM), a novel tyrosine kinase inhibitor, has been applied in treating various cancers. In the present study, the binding mechanism of APM with bovine serum albumin (BSA) was studied by making use of various spectroscopic and theoretical calculation approaches to provide theoretical support for further studying its pharmacokinetics and metabolism. The results from fluorescence experiments showed that the quenching mechanism of BSA induced by APM was static quenching and the APM-BSA complex with the stoichiometry of 1:1 was formed during binding reaction. Moreover, the findings also showed that the binding process of APM to BSA was spontaneous and enthalpy-driven, and the mainly driving forces were hydrogen bonding, van der Waals as well as hydrophobic interactions. From the outcomes of the competitive experiments, it can be found that the binding site was primarily nestled in sub-domain IIIA of BSA (site II) which was in line with the results of molecular docking. An appreciable decline in α-helix content of BSA can be observed from the FT-IR data, meaning that the conformational change of BSA occurred after binding with APM, this phenomenon can be corroborated by the results of UV-vis, synchronous fluorescence and 3D fluorescence studies. Furthermore, the effect of some metal ions (e.g. K+, Co2+, Ni2+, Fe3+) on the binding constant of APM to BSA was explored.Communicated by Ramaswamy H. Sarma.

Pressure-Driven Transformation of CsPbBrI2 Nanoparticles into Stable Nanosheets in Solution through Self-Assembly.

Very recently, two-dimensional (2D) perovskite nanosheets (PNSs), taking the advantages of perovskite as well as the 2D structure properties, have received an enormous level of interest throughout the scientific community. In spite of this incredible success in perovskite nanocrystals (NCs), self-assembly of many nanostructures in metal halide perovskites has not yet been realized, and producing highly efficient red-emitting PNSs remains challenging. In this Letter, we show that by using CsPbBrI2 perovskite nanoparticles (NPs) as a building block, PNSs can emerge spontaneously under high ambient pressure via template-free self-assembly without additional complicated operation. It is found that the formation of PNSs is ascribed to the high pressure that provides the driving force for the alignment of NPs in solution. Because of the disappearance of the grain boundaries between the adjacent NPs and increased crystallinity, these PNSs self-assembled from NPs exhibit enhanced properties compared to the initial NPs, including higher PL intensity and remarkable chemical stability toward light and water.

Insights on the interaction mechanism of brigatinib to human α-1-acid glycoprotein: Experimental and computational approaches.

Brigatinib, a multi-target kinase inhibitor, is primarily used to treat anaplastic lymphoma kinase (ALK)-positive patients with advanced non-small cell lung cancer (NSCLC) who have previously received crizotinib or are resistant to crizotinib. In this study, we focused on elucidating the interaction mechanism between brigatinib and human alpha-1-acid glycoprotein (HAG) through experimental and computational approaches. Steady-state fluorescence and UV-vis spectroscopy measurements revealed that brigatinib could quench the intrinsic fluorescence of HAG in a static quenching manner and formed the brigatinib-HAG complex with the stoichiometric ratio of 1:1. The findings revealed that brigatinib had a stronger affinity on HAG due to higher binding constant of 2.91 × 105 M-1 at 298 K. It can be proved from thermodynamic parameter analysis that brigatinib spontaneously bound to HAG in the means of enthalpy driven, the main forces for stabilizing brigatinib-HAG complexes were hydrogen bonding and hydrophobic interactions. The experimental results also indicated that the binding interaction induced micro-environmental changes around tryptophan residues and the alteration in secondary structure of HAG. The presence of metal ions like Mg2+, Zn2+, Ca2+, Ni2+ and Co2+ affects the binding interaction and thus change the therapeutic efficacy of brigatinib. Molecular docking results suggested that brigatinib was embedded to the hydrophobic cavity of HAG. The experimental and computational results certified that hydrogen bonding and hydrophobic interaction as well as electrostatic energy and van der Waals forces plays a leading role in the binding process.

Insight into the binding behavior of ceritinib on human α-1 acid glycoprotein: Multi-spectroscopic and molecular modeling approaches.

Ceritinib is a second-generation anaplastic lymphoma kinase (ALK) inhibitor for mainly treating non-small cell lung cancer (NSCLC). This investigation focused on to clarify in detail the binding behavior between human α-1 acid glycoprotein (HAG) and ceritinib by means of multi-spectroscopic and molecular modeling approaches. Fluorescence data obtained at four different temperatures indicated ceritinib quenched the endogenous fluorescence of HAG by a static quenching mechanism. Based on the Kb value at 105 M-1 level, it can be inferred that the binding affinity between both is strong. From findings of thermodynamic parameter analysis, the competitive experiments with ANS and sucrose as well as molecular dynamic (MD) simulation, it can be inferred that hydrophobicity, hydrogen bonding, van der Waals forces as well as electrostatic interactions exist in the binding interaction between ceritinib and HAG. The findings from UV absorption, circular dichroism, and synchronous fluorescence spectroscopy indicated that the change in the microenvironment around the protein structure, secondary structure and tryptophan residues occurred after interaction with ceritinib. The data from FRET analysis confirmed that the non-radiative energy transfer between the two existed and the binding distance between the acceptor (ceritinib) and donor (HAG) was 2.11 nm. Meantime, the influence of Ca2+, Cu2+, Ni2+, Co2+, and Zn2+ ions on the binding interaction of ceritinib with HAG were obvious, especially Zn2+ ion.

Assessment on the binding affinity between ritonavir with model transport protein: a combined multi-spectroscopic approaches with computer simulation.

The binding affinity between ritonavir (RTV) and model transport protein, BSA was assessed through multi-spectroscopic approaches and computer simulation. The findings revealed RTV statically quenched the fluorescence of BSA and formed the 1:1 RTV-BSA complex with the binding constant (Kb) of 1.06 × 103 ∼ 5.08 × 103 M-1 under the studied temperatures (298 ∼ 310 K). During the interaction of RTV with BSA, the hydrogen bonds and van der Waals forces acted as predominant function while the hydrophobicity played an assistant function. Molecular modeling further verified the result obtained from the competitive binding experiments, RTV preferentially fit into in the sub-domain IIIA of BSA. The perturbation in the secondary structures of BSA upon acting with RTV was observed from IR results, whereas synchronous and 3D fluorescence spectral findings unraveled the slight change in the hydrophobicity surrounding Tyr and Trp residues.Communicated by Ramaswamy H. Sarma.

Assessment on the binding characteristics of dasatinib, a tyrosine kinase inhibitor to calf thymus DNA: insights from multi-spectroscopic methodologies and molecular docking as well as DFT calculation.

The binding characteristics of calf thymus DNA (ct-DNA) with dasatinib (DSTN), a tyrosine kinase inhibitor was assessed through multi-spectroscopic methodologies and viscosity measurement combined with molecular docking as well as DFT calculation to understand the binding mechanism, affinity of DSTN onto ct-DNA, effect of DSTN on ct-DNA conformation, and among others. The results confirmed DSTN bound onto ct-DNA, leading to forming the DSTN-ct-DNA complex with the binding constant of 4.82 × 103 M-1 at 310 K. DSTN preferentially inserted to the minor groove of ct-DNA with rich A-T region, that was the binding mode of DSTN onto ct-DNA was groove binding. The enthalpic change (ΔH0) and entropic change (ΔS0) during the binding process of DSTN with ct-DNA were 128.9 kJ mol-1 and 489.2 J mol-1 K-1, respectively, confirming clearly that the association of DSTN with ct-DNA was an endothermic process and the dominative driven-force was hydrophobic interaction. Meanwhile, the results also indicated that there was a certain extent of electrostatic force and hydrogen bonding, but they maybe play an auxiliary role. The CD measurement results confirmed the alteration in the helical configuration of ct-DNA but almost no change in the base stacking after binding DSTN. The results revealed that there was the obvious change in the conformation, the dipole moment, and the atomic charge distribution of DSTN in the B-DNA complexes, compared with free DSTN, to satisfy the conformational adaptation. From the obtained fronitier molecular orbitals of DSTN, it can be inferred that the nature of DSTN alters with the change of the environment around DSTN. Communicated by Ramaswamy H. Sarma.

Preparation and performance of Cu2O/TiO2 nanocomposite thin film and photocatalytic degradation of Rhodamine B.

A constant current electrodeposition approach was employed to prepare Cu2O/TiO2 nanocomposite thin film. X-ray diffraction (XRD), X-ray photoelectron spectroscopy (XPS), scanning electron microscopy (SEM), Raman, ultraviolet visible light spectrophotometer (UV-Vis), and photoluminescence (PL) measurements were used to characterize and analyze the thin film microstructure, surface morphology, and photoelectric properties. The effect of annealing treatment on the thin film properties is discussed. The response surface methodology (RSM) was employed to optimize the Rhodamine B (RhB) photocatalytic degradation by thin films, and the quadratic multinomial mathematical model was established. The photocatalytic degradation process of RhB was also studied. The results indicate that the prepared Cu2O thin film was of high purity, with a (111) crystal plane preferred orientation. The average particle diameter was approximately 100-200 nm, and the absorbing boundary was approximately 600 nm. After annealing treatment, the absorbing boundary and open-circuit voltage increased, and Cu2O thin film exhibited an obvious absorbance response in the visible-light range. The established model has better fitness and higher reliability, and the R2 value of established quadratic model is 0.9818. The optimal degradation conditions were obtained by RSM. Under optimum conditions, the RhB degradation rate could reach 98.4% in 3 h and the total organic carbon (TOC) removal rate was 48.2%. Recycling results reveal that RhB degradation rate can still reach 94.5% after eight cycles.