Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Regarding Emitter Positioning for Nanoflow Electrospray Ionization

ABSTRACT: BSA tryptic peptides were infused using nanoflow electrospray. Each raw file represents a different emitter position.

INSTRUMENT(S): Orbitrap Ascend

ORGANISM(S): Bos Taurus (ncbitaxon:9913)

SUBMITTER: Joshua Coon

PROVIDER: MSV000100165 | MassIVE | Tue Dec 09 12:43:00 GMT 2025

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Electrospray ionization in concentrated acetonitrile vapor improves the performance of mass spectrometry for proteomic analyses

Project description:Suppressing the background interferences and enhancing the analyte signals are long-term goals in high performance electrospray ionization mass spectrometry (ESI-MS) analyses. We observed that performing electrospray in the presence of a concentrated acetonitrile atmosphere suppresses background interferences and enhances peptide signals. An enclosed nanoESI source was utilized to provide a stable atmosphere of concentrated acetonitrile vapor for high performance ESI-MS analyses. The median MS signal intensity increased by 5 times for a set of 23 BSA tryptic peptides in direct nanoESI-MS analysis. Further, the number of reproducibly and precisely quantified peptides could be improved 67% in six replicate label-free quantitative proteome analyses by this strategy.

2017-01-04 | PXD005132 | Pride

Assessment of Immunological Responses to Water Electrospray: A Novel Non-Chemical Biocide for Safe Disinfection

Project description:Water electrospray is small charged droplets generated by a laboratory-designed prototype module. Extensive investigations have explored its physical properties and identified a potential non-chemical biocide against air-borne pathogens. However, since humans can inhale water electrospray particles through breath, humans' safety and potential toxicity warrant investigation. Hence, to offer insights into the effect of water electrospray on humans, we analyzed the immunopathological response to water electrospray using a nasal challenge mouse model. For this, we accessed the fundamental immune responses following the water electrospray intranasal challenge by comparing its effect with sodium hypochlorite, a biocidal agent with known toxicity. Our results indicate that water electrospray did not induce pathological immune reactions: challenged mice did not exhibit body weight loss and increased inflammatory cytokine production. Furthermore, histopathological analysis revealed that water electrospray did not damage the lung tissue, whereas sodium hypochlorite–treated mice showed significant lung tissue damage with signs of neutrophils and eosinophils infiltration. Finally, transcriptomic analysis on lung tissue confirmed the absence of pathological immune response in water electrospray-treated mice compared with sodium hypochlorite–treated mice. Together, we provide evidence that water electrospray is a safe technology for its use in disinfecting air-borne pathogens with little or no effect on immune system activation at the preclinical level.

2025-04-02 | GSE262972 | GEO

Ethylene glycol improves electrospray ionization

Project description:We evaluated a number of compounds as LC additives to modify the electrospray response and found that ethylene glycol was capable of enhancing nESI response by a factor of twofold on average. This result was comparable to DMSO.

2017-07-14 | PXD004919 | Pride

Precision-Engineered Nano-Electrospray Emitters Enhance Ionization Efficiency for Trap-Assisted Direct Infusion Mass Spectrometry: Application in Plasma Alzheimer’s Disease Proteomics

Project description:Shotgun direct infusion mass spectrometry (DI-MS) enables high-throughput proteomics. Yet, its performance critically depends on nanospray emitter quality. We present here precision-engineered nanospray emitters with an optimized 4-degree emitter tip angle, designed for sensitive, reproducible, user friendly, and compatible across mass spectrometry platforms that demonstrated enhanced ionization efficiency and spray stability, showing a 21-fold improvement in protein identification rates compared to commercial designs. Using both digested HeLa cell protein extracts and plasma samples from Alzheimer's disease (AD) patients and controls, where the 14 most high-abundant proteins were depleted, we performed a comprehensive DI-MS protein identification and precise quantification using both Orbitrap Exploris 480 (OE480) and Orbitrap Astral mass spectrometers. We consistently identified and quantified over 160 proteins in AD plasma samples in 4 min DI-MS runs, with superior reproducibility (CV < 15%) and sensitivity on the Orbitrap Astral. Our analysis revealed several unreported disease-associated protein signatures, while confirming known AD biomarkers, with C5, C4BPA, and FAM135B as the protein combination with the highest potential as AD plasma biomarkers for the detection of the disease. The enhanced performance of these standardized engineered nanospray emitters over the established DI-MS workflow establishes a robust and scalable platform for high-throughput clinical proteomics.

2025-07-31 | PXD061620 | Pride

Precision-Engineered Nano-Electrospray Emitters Enhance Ionization Efficiency for Trap-Assisted Direct Infusion Mass Spectrometry: Application in Plasma Alzheimer’s Disease Proteomics

Project description:Shotgun direct infusion mass spectrometry (DI-MS) enables high-throughput proteomics. Yet, its performance critically depends on nanospray emitter quality. We present here precision-engineered nanospray emitters with an optimized 4-degree emitter tip angle, designed for sensitive, reproducible, user friendly, and compatible across mass spectrometry platforms that demonstrated enhanced ionization efficiency and spray stability, showing a 21-fold improvement in protein identification rates compared to commercial designs. Using both digested HeLa cell protein extracts and plasma samples from Alzheimer's disease (AD) patients, and controls, where the 14 most high-abundant proteins were depleted, we performed a comprehensive DI-MS protein identification and precise quantification using both Orbitrap Exploris 480 (OE480) and Orbitrap Astral mass spectrometers. We consistently identified and quantified over 160 proteins in AD plasma samples in 4 min DI-MS runs, with superior reproducibility (CV < 15%) and sensitivity on the Orbitrap Astral. Our analysis revealed several unreported disease-associated protein signatures, while confirming known AD biomarkers, with C5, C4BPA, and FAM135B as the protein combination with the highest potential as AD plasma biomarkers for the detection of the disease. The enhanced performance of these standardized engineered nanospray emitters over the established DI-MS workflow establishes a robust and scalable platform for high-throughput clinical proteomics.

2025-07-20 | PXD061608 | Pride

Nanobubbles in Electrospray Ionization Mass Spectrometry.

Project description: Not available

| S-EPMC11948179 | biostudies-literature

Influence of Albumin Concentration on Surface Characteristics and Cellular Responses in the Pre-Incubation of Multi-Walled Carbon Nanotubes

Project description:Due to the characteristics of multi-walled carbon nanotubes (MWCNTs) to aggregate and bind non-specifically, attempts have been made to inhibit their aggregation and increase their dispersion stability for biomedical applications by coating with bovine serum albumin (BSA). However, BSA concentration has not been studied in detail in terms of cellular response. To investigate the surface proteins formed in 10% fetal bovine serum cell culture media depending on the BSA concentration used to stabilize MWCNTs and to correlate the cellular responses with BSA concentration, we performed nanoflow liquid chromatography–electrospray ionization–tandem mass spectrometry analysis to quantify proteins of the protein corona (PC) and of A549 cells. Results showed that increasing the concentration of pre-incubated BSA changed the composition ratio of the proteins of the PCs adsorbed on the MWCNTs and also decreased the cellular uptake of A549 cells treated with BSA-coated MWCNTs. In the proteomic analysis, proteins related to the ribosome, ribosome biogenesis in eukaryotes, and oxidative phosphorylation pathways were downregulated in the low concentration BSA-treated cell groups, while proteins related to the mRNA surveillance pathway were downregulated in the high-BSA-concentration cell groups. Moreover, circular dichroism and Fourier-transform infrared spectroscopy results showed that the α-helix structure, a secondary structure of the adsorbed proteins, increased as a function of BSA concentration. Taken together, BSA concentration affects the adsorption and secondary structure of PCs on MWCNTs, which in turns affect their intracellular behavior. Our results may provide insight for the design of modification methods to increase the biocompatibility of MWCNTs.

2024-10-21 | PXD052226 | Pride

Desorption electrospray ionization-mass spectrometry of proteins.

Project description: Not available

| S-EPMC3176668 | biostudies-literature

Electrothermal supercharging of proteins in native electrospray ionization.

Project description: Not available

| S-EPMC3328611 | biostudies-literature

Deep-ultraviolet laser ablation electrospray ionization mass spectrometry.

Project description: Not available

| S-EPMC6422691 | biostudies-literature