Highly stable all-inorganic perovskite quantum dot/polymethylsilsesquioxane aerogel (CsPbBr3/PMSQ AG) composites were first produced using two-step hot-injection and encapsulation processes by embedding green-emitting CsPbBr3 PQDs into modified hydrophobic mesoporous silica AGs. The unique structure of the composites not only considerably enhances the chemical stability of CsPbBr3 PQDs against moisture, humidity, and blue-light irradiation in air but also prevents anion exchange reactions during light-emitting diode (LED) manufacturing processes. In addition, the composition-optimized CsPbBr3/PMSQ AG exhibited excellent stability when soaked in water for more than 14 days and retained half of its initial intensity. Finally, white LED devices were fabricated by combining a blue-emitting GaN-based chip, green-emitting CsPbBr3/PMSQ AG, and red-emitting K2SiF6Mn4+ phosphors.The poor ultraviolet (UV) resistance and insufficient solvent compatibility are challenges for long-term storage and service of oil-water separation materials in practical applications. Herein, a superhydrophobic/superoleophilic surface with nano- to microscale hierarchical structures was formed spontaneously on robust microcapsules (MCs) via in situ polymerization and a sol-gel surface treatment. The resultant MCs possessed superior UV-resistant and solvent-proof superhydrophobicity. The water contact angles (WCAs) of the MC coating remained above 160° and the sliding angles (SAs) were below 3° after 9 days of UV aging test or 20 days of nonpolar and polar aprotic solvent immersion tests. More interestingly, these MCs can be used to separate the oil phase from its aqueous emulsion effectively, achieving a high and reusable separation efficiency with over 90% oil purity after 10 cycles of filtrations even after 13 days of UV aging. Therefore, these novel MCs will exhibit effective oil-water separation performance, superior chemical stability, outstanding reusability, and long-term storage stability for promising practical applications.Measurement of monoclonal antibodies (M-proteins) plays an important role in the diagnosis and treatment monitoring of multiple myeloma. Currently available M-protein assays have several limitations, particularly because of their lack of sensitivity and propensity to therapeutic antibody (t-mAb) interference. A previously described mass spectrometry method termed monoclonal immunoglobulin rapid accurate mass measurement (miRAMM) is more sensitive than current clinical tests and can provide a solution for resolving t-mAb interferences. see more However, the original miRAMM workflow is too complex for the throughput needed to analyze a large number of samples. Here, we describe a high-throughput liquid chromatography-high-resolution mass spectrometry (HT-LC-HRMS) approach that employs a fully automated immunocapture step, significantly improved immunoglobulin recovery, simplified chromatography, and high throughput (HT) data processing. In this HT-LC-HRMS approach, raw spectra of the peaks eluting from the LC column during the predefined time period are automatically deconvoluted without the need to identify and monitor the retention time of each patient-specific M-protein. The deconvoluted peak heights of M-protein and therapeutic antibody light chain are conveniently used for quantitation. With the total LC-HRMS measurement time being only 11.0 min, this method was able to differentiate between the M-protein and elotuzumab mass signatures in 91 out of 92 (98.9%) multiple myeloma serum samples tested. The single interference case was resolved using the mass signature of a heavy chain. In addition to resolving t-mAb interference, the developed assay has a 25-fold improvement in sensitivity over immunofixation electrophoresis and can potentially provide an objective tracking of M-proteins in patients with complete response.Trimethylation enhancement using diazomethane (TrEnDi) is a derivatization technique that significantly enhances the signal intensity of glycerophospholipid species in mass spectrometry (MS) and tandem mass spectrometry (MS/MS) analyses. Here, we describe a novel apparatus that is able to conduct in situ TrEnDi (iTrEnDi) by generating and immediately reacting small amounts of gaseous diazoalkane with analyte molecules. iTrEnDi allows complete and rapid methylation of phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA), and sphingomyelin (SM) in a safe manner by removing any need for direct handling of dangerous diazoalkane solutions. iTrEnDi-modified PC ([PCTr]+) and PE ([PETr]+) showed similar sensitivity enhancements and fragmentation patterns compared to our previously reported methodology. iTrEnDi yielded dimethylated PA ([PATr]), which exhibited dramatically improved chromatographic behavior and a 14-fold increase in liquid chromatography MS (LCMS) sensitivity compared to unmodified PA. In comparison to in-solution-based TrEnDi, iTrEnDi demonstrated a modest decrease in sensitivity, likely due to analyte losses during handling. However, the enhanced safety benefits of iTrEnDi coupled with its ease of use and capacity for automation, as well as its accommodation of more-reactive diazoalkane species, vastly improve the accessibility and utility of this derivatization technique. Finally, as a proof of concept, iTrEnDi was used to produce diazoethane (DZE), a more-reactive diazoalkane than diazomethane. Reaction between DZE and PC yielded ethylated [PCTr]+, which fragmented via MS/MS to produce a high-intensity characteristic fragment ion, enabling a novel and highly sensitive precursor ion scan.Abnormal glycan structures are valuable biomarkers for disease states; the development of glycan-specific binders is thereby significantly important. However, the structural homology and weak immunogenicity of glycans pose major hurdles in the evolution of antibodies, while the poor availability of complex glycans also has extremely hindered the selection of anti-glycan aptamers. Herein, we present a new approach to efficiently screen aptamers toward specific glycans with a complex structure, using a glycosylated peptide as a scaffold. In this method, using peptide-imprinted magnetic nanoparticles (MNPs) as a versatile platform, a glycopeptide tryptically digested from a native glycoprotein was selectively entrapped for positive selection, while a nonglycosylated analogue with an identical peptide sequence was synthesized for negative selection. Alternating positive and negative selection steps were carried out to guide the directed evolution of glycan-binding aptamers. As proof of the principle, the biantennary digalactosylated disialylated N-glycan A2G2S2, against which there have been no antibodies and lectins so far, was employed as the target.