Characterization and Hydrogenation Removal of Acid-Soluble Oil in Ionic Liquid Catalysts for Isobutane Alkylation

Acid-soluble oil (ASO) was produced during isobutane alkylation catalyzed by chloroaluminate ionic liquids (CAILs). However, the ASO composition characterizations and deactivated CAIL regeneration pathway were not clarified. In this work, a series of characterizations (elemental analysis and infrared, ultraviolet, and mass spectroscopy) were performed to reveal the ASO composition. The result showed that ASO contained numerous conjugated cycloolefins with various alkyl substituents and a few O1–O5 compounds. The activity index (AI) value of fresh CAILs was 1.74 and decreased to 1.18 with the addition of 9.09 wt % ASO because the [Al2Cl7]− anion in CAILs was complexed by CC and CO bonds in ASO. The hydrogenation regeneration of deactivated CAILs on the Pd/C catalyst was studied. The AI value of regenerated CAILs increased to 1.45 because unsaturated bonds in ASO were hydrogenated to saturation. Recovery of unsaturated hydrocarbons followed the order benzene > 1-methylcyclopentene > pentamethylcyclopentadiene. This work demonstrated that low ASO recovery was attributed to the partial occupation of the π-electron of unsaturated bonds by the [Al2Cl7]− anion

Flow-Enhanced Flexible Microcomb Printing of Organic Solar Cells

Scalable and roll-to-roll compatible processing methods have become pressing needs to transfer organic solar cells (OSCs) to realistic energy sources. Herein a new fabrication method of flexible microcomb printing is proposed. The microcomb is based on a PET sheet micromachined into comb teeth by a laser marker. A computational fluid mechanics simulation shows that the fluid flow around the microcomb teeth induces high shear as well as extensional strain rates, which enhance the molecular alignment and lateral mass transport. The PTQ10:Y6-BO OSCs printed by the flexible microcomb demonstrate a substantially increased degree of crystallinity and phase separation with a suitable domain size. Devices printed by the flexible microcomb in air achieve PCEs of up to 15.93%, higher than those of control devices spin-coated in the N2 glovebox. The flexibility of the PET film makes the microcomb teeth contact directly with the substrate without a suspended liquid meniscus, thus facilitating printing on soft or curved substrates. Printing of flexible OSCs and large-area devices are demonstrated. The flexible OSCs exhibit PCEs of up to 13.62%, which is the highest for flexible OSCs made by scalable printing techniques to date. These results make flexible microcomb printing a feasible and promising strategy toward the manufacture of efficient OSCs

Reaction Behaviors and Mechanism of Isobutane/Propene Alkylation Catalyzed by Composite Ionic Liquid

Alkylation performance of isobutane with propene catalyzed by composite ionic liquid (CIL) was deeply investigated. Critical components of alkylate were C7 isoparaffins, which were mainly 2,3-dimethylpentane and 2,4-dimethylpentane. The optimal reaction conditions were as follows: reaction temperature of 15 °C, reaction time of 5 s, stirring rate of 1500 rpm, IL/HC ratio of 1.0, and I/O ratio of 68. Under these conditions, the yield of C7 isoparaffins was 78.9 wt %, and the research octane number of alkylate was 86.2. The reaction mechanism and pathway of isobutane/propene alkylation were proposed on the basis of component distribution. C7 isoparaffins were mainly from direct alkylation, and C8 isoparaffins were mainly from disproportionation. Compared with traditional concentrated sulfuric acid and hydrofluoric acid catalysts, more direct alkylation and less self-alkylation occurred, and the yield of propane was much lower when CIL was used. It was also proved that propene could be used in the CIL-catalyzed alkylation industrial unit due to the low propane production

Organic Photovoltaics Printed via Sheet Electrospray Enabled by Quadrupole Electrodes

Developing manufacturing methods that are scalable and compatible with a roll-to-roll process with low waste of material has become a pressing need to transfer organic photovoltaics (OPVs) to a viable renewable energy source. For this purpose, various spray printing methods have been proposed. Among them, electrospray (ES) is an attractive option due to its negligible material waste, tunable droplet size, and tolerance to the substrate defects and roughness. Conventional ES with a circular spray footprint often makes the droplets well separated and unlikely to merge, giving rise to “coffee rings” which cause a rough and flawed film morphology. Here, a quadrupole electrode is introduced to generate a compressing electric field that squeezes the conical ES profile into the shape of a thin sheet. The numerical simulation and experimental data of the trajectories of sprayed droplets show that the quadrupole apparatus can effectively increase the long axis to short axis ratio of the oval spray footprint and hence bring droplets closer to each other and make the merging more likely for the deposited droplets. By promoting the merging of droplets, individual coffee rings are also suppressed. Thus, the quadrupole ES offers untapped opportunities for effectively reducing voids and improving the flatness of the ES-printed active layer. The devices with a PM6:N3 active layer printed by the sheet ES exhibited the highest power conversion efficiency (PCE) of up to 15.98%, which is a noticeable improvement over that (14.85%) of counterparts fabricated by a conventional conical ES. This is the highest PCE reported for ES-printed OPVs and is one of the most efficient spray-deposited OPVs so far. In addition, the all-spray-printed devices reached a PCE of 14.55%, which is also among the most efficient all-spray-printed OPVs

Identification of Missing Proteins Defined by Chromosome-Centric Proteome Project in the Cytoplasmic Detergent-Insoluble Proteins

Finding protein evidence (PE) for protein coding genes is a primary task of the Phase I Chromosome-Centric Human Proteome Project (C-HPP). Currently, there are 2948 PE level 2–4 coding genes per neXtProt, which are deemed missing proteins in the human proteome. As most samples prepared and analyzed in the C-HPP framework were focusing on detergent soluble proteins, we posit that as a natural composition the cytoplasmic detergent-insoluble proteins (DIPs) represent a source of finding missing proteins. We optimized a workflow and separated cytoplasmic DIPs from three human lung and three human hepatoma cell lines via differential speed centrifugation. We verified that the detergent-soluble proteins (DSPs) could be sufficiently depleted and the cytoplasmic DIP isolation was partially reproducible with Spearman <i>r</i> > 0.70 according to two independent SILAC MS experiments. Through label-free MS, we identified 4524 and 4156 DIPs from lung and liver cells, respectively. Among them, a total of 23 missing proteins (22 PE2 and 1 PE4) were identified by MS, and 18 of them had translation evidence; in addition, six PE5 proteins were identified by MS, three with translation evidence. We showed that cytoplasmic DIPs were not an enrichment of transmembrane proteins and were chromosome-, cell type-, and tissue-specific. Furthermore, we demonstrated that DIPs were distinct from DSPs in terms of structural and physical–chemical features. In conclusion, we have found 23 missing proteins and 6 PE5 proteins from the cytoplasmic insoluble proteome that is biologically and physical-chemically different from the soluble proteome, suggesting that cytoplasmic DIPs carry comprehensive and valuable information for finding PE of missing proteins. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium with the data set identifier PXD001694

Finding Missing Proteins from the Epigenetically Manipulated Human Cell with Stringent Quality Criteria

The chromosome-centric human proteome project (C-HPP) has made great progress of finding protein evidence (PE) for missing proteins (PE2–4 proteins defined by the neXtProt), which now becomes an increasingly challenging field. As a majority of samples tested in this field were from adult tissues/cells, the developmental stage specific or relevant proteins could be missed due to biological source availability. We posit that epigenetic interventions may help to partially bypass such a limitation by stimulating the expression of the “silenced” genes in adult cells, leading to the increased chance of finding missing proteins. In this study, we established <i>in vitro</i> human cell models to modify the histone acetylation, demethylation, and methylation with near physiological conditions. With mRNA-seq analysis, we found that histone modifications resulted in overall increases of expressed genes in an even distribution manner across different chromosomes. We identified 64 PE2–4 and six PE5 proteins by MaxQuant (FDR < 1% at both protein and peptide levels) and 44 PE2–4 and 7 PE5 proteins by Mascot (FDR < 1% at peptide level) searches, respectively. However, only 24 PE2–4 and five PE5 proteins in Mascot, and 12 PE2–4 and one PE5 proteins in MaxQuant searches could, respectively, pass our stringently manual spectrum inspections. Collectively, 27 PE2–4 and five PE5 proteins were identified from the epigenetically modified cells; among them, 19 PE2–4 and three PE5 proteins passed FDR < 1% at both peptide and protein levels. Gene ontology analyses revealed that the PE2–4 proteins were significantly involved in development and spermatogenesis, although their chemical–physical features had no statistical difference from the background. In addition, we presented an example of suspicious PE5 peptide spectrum matched with unusual AA substitutions related to post-translational modification. In conclusion, the epigenetically manipulated cell models should be a useful tool for finding missing proteins in C-HPP. The mass spectrometry data have been deposited to the iProx database (accession number: IPX00020200)

Finding Missing Proteins from the Epigenetically Manipulated Human Cell with Stringent Quality Criteria

The chromosome-centric human proteome project (C-HPP) has made great progress of finding protein evidence (PE) for missing proteins (PE2–4 proteins defined by the neXtProt), which now becomes an increasingly challenging field. As a majority of samples tested in this field were from adult tissues/cells, the developmental stage specific or relevant proteins could be missed due to biological source availability. We posit that epigenetic interventions may help to partially bypass such a limitation by stimulating the expression of the “silenced” genes in adult cells, leading to the increased chance of finding missing proteins. In this study, we established <i>in vitro</i> human cell models to modify the histone acetylation, demethylation, and methylation with near physiological conditions. With mRNA-seq analysis, we found that histone modifications resulted in overall increases of expressed genes in an even distribution manner across different chromosomes. We identified 64 PE2–4 and six PE5 proteins by MaxQuant (FDR < 1% at both protein and peptide levels) and 44 PE2–4 and 7 PE5 proteins by Mascot (FDR < 1% at peptide level) searches, respectively. However, only 24 PE2–4 and five PE5 proteins in Mascot, and 12 PE2–4 and one PE5 proteins in MaxQuant searches could, respectively, pass our stringently manual spectrum inspections. Collectively, 27 PE2–4 and five PE5 proteins were identified from the epigenetically modified cells; among them, 19 PE2–4 and three PE5 proteins passed FDR < 1% at both peptide and protein levels. Gene ontology analyses revealed that the PE2–4 proteins were significantly involved in development and spermatogenesis, although their chemical–physical features had no statistical difference from the background. In addition, we presented an example of suspicious PE5 peptide spectrum matched with unusual AA substitutions related to post-translational modification. In conclusion, the epigenetically manipulated cell models should be a useful tool for finding missing proteins in C-HPP. The mass spectrometry data have been deposited to the iProx database (accession number: IPX00020200)