News from LabRulezICPMS Library - Week 12, 2026

Our Library never stops expanding. What are the most recent contributions to LabRulezICPMS Library in the week of 16th March 2026? Check out new documents from the field of spectroscopy/spectrometry and related techniques!

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This week we bring you application notes by Metrohm, Shimadzu, Thermo Fisher Scientific and Waters Corporation!

1. Metrohm: Soil analysis with NIR spectroscopy

Multiparameter determination of soil in a few seconds

• Application note
• Full PDF for download

Soil is a complex matrix made of organic and inorganic mineral matter, water, and air. The organic material ranges from decomposed and stable humus to fresh particulate residues from different sources [1]. Texture affects soil behavior (e.g., water holding capacity, nutrient retention and supply, drainage, and nutrient leaching [2]) and depends on the proportion by weight of the sand, silt, and clay it contains. Cationexchange capacity (CEC), a measure of the ability to hold positively charged ions, influences soil structure stability, nutrient availability, pH, and its reaction to fertilizers and other ameliorants. The main ions associated with CEC in soils are Ca2+, Mg2+, Na+ , and K + [3]. Soil pH directly influences the availability of nutrients to plants, microbial activity, and overall soil health, affecting plant growth, crop yields, and the sustainability of agricultural practices. This study describes how organic matter content, pH value, silt, clay and sand content, exchangeable calcium and magnesium, and limestone content were measured in soil in seconds by using near-infrared spectroscopy (NIRS).

EXPERIMENTAL EQUIPMENT

Air-dried samples of soil [4] were measured on a Metrohm NIR Analyzer. All measurements were performed in reflection mode (1000–2250 nm) using the large cup accessory. The samples were measured in rotation to collect spectral data from several areas. Spectral averaging of signals from several spots helped to reduce sample inhomogeneity. Metrohm software was used for all data acquisition and prediction model development.

CONCLUSION

This Application Note displays the benefits of using NIR spectroscopy for soil analysis. All the presented soil quality parameters can be measured simultaneously in only a few seconds. Compared to other conventional methods (Table 1), near-infrared spectroscopy soil analysis requires no sample preparation nor solvents. This ultimately leads to a reduction in workload and related costs, as well as keeping lab personnel safer.

2. Shimadzu: Observation of Shock Waves Using the Schlieren Method with the HPV-X3

• Application note
• Full PDF for download

User Benefits

• HPV-X3 offers three times the resolution of conventional models, enabling high-speed imaging at much higher resolutions.
• With a maximum frame rate of 20 Mfps, the HPV-X3 is well-suited for observing high-speed phenomena such as shock waves

Shock waves are characterized by abrupt changesin pressure and density and are generated when an object travels faster than the speed of sound or during explosive phenomena. They are important research subjects in fields such as aerospace and fluid dynamics. In particular, accurately characterizing the structure and temporal evolution of shock waves generated around projectiles is a crucial issue directly related to vehicle design, behavior prediction, and safety evaluation. Optical techniques capable of detecting minute changes in refractive index are effective for visualizing such phenomena. Among these, the Schlieren method is widely used to visualize density variations in fluids. ¹⁾ 

In this paper, the HPV-X3 high-speed video camera (Fig. 1), which provides three times the resolution of conventional models, was used to observe shock waves generated by a pellet launched from a gas gun using the Schlieren method.

Imaging System 

The pellet shown at the center of Fig. 2 was placed in the firing chamber of the gas gun, sandwiched between two plastic holders. The holders were used to position the pellet in the firing chamber; after firing, the holders fell away, allowing only the pellet to be captured by the camera. 

The imaging system is detailed in Table 1, the imaging conditions are shown in Table 2, and the experimental setup is shown in Fig. 3. Light from the laser source was reflected by Concave mirror (1) and collimated between Concave mirrors (1) and (2). The HPV-X3 captured images of shock waves generated along the projectile path through a mirror and a knife-edge. 

The experiment was conducted twice: in the first trial, two rubber bands were placed in the projectile path; in the second trial, an obstacle with ten circular holes (Fig. 4) was placed in the path. This allowed us to observe phenomena such as fragmentation and shock wave reflection.

Conclusion 

Using the HPV-X3 high-speed video camera, shock waves generated by pellets fired from a gas gun were observed using the Schlieren method. This approach enabled close observation of phenomena, including shock waves generated as the pellet passed through or was reflected by rubber bands placed in the projectile path, as well as pellet fragmentation by impact with an obstacle and the subsequent generation of shock waves from each fragment. 

The HPV-X3 high-speed video camera has three times the resolution of the previous, HPV-X2, model and is well-suited for detailed observation of high-speed phenomena such as shock waves.

3. Thermo Fisher Scientific: Raman Spectroscopy: Deciphering the Structural Dynamics of 2D Semiconductors

• Application note
• Full PDF for download

Semiconductors form the foundation of all modern electronics. As industries constantly seek to make their technological devices even smaller and more efficient, and manufacturers continue to strive for more compact device architectures, the key to future develops may prove to be new, thin film materials. Thin film or twodimensional (2D) semiconductors have unique properties and perform robustly even at monolayer thicknesses, allowing for complex electronic device performance at extremely small scale.¹ For example, the current silicon “2 nm” transistors used in the semiconductor industry have channel lengths of 10+ nm. Studies on 2D semiconductor transistors, especially MoS₂, show promising scalability to physical channel lengths below a 5 nm threshold—less than half the size of current transistors.¹ These materials have very well-defined crystal structures which make them excellent candidates for characterization through Raman spectroscopy. A common class of these materials is the transition metal dichalcogenide (TMDC) family such as molybdenum disulfide (MoS₂).², ³ 2D semiconductors, like TDMCs, are characterized by two major structural elements: the in-plane lattice bonds and out-of-plane van der Waals (vdW) forces that bind the stacked layers of crystalline monolayers.²

Crystal Structure and Raman Signal 

A naturally formed sample of MoS₂ is studied here using the Thermo Scientific DXR3xi Raman Imaging Microscope with a 455 nm excitation laser. The MoS₂ is manually exfoliated to thin the crystals from bulk form down to a two-dimensional, thin film layer.³ This creates a very simple crystalline structure with simple vibrational modes. Indeed, MoS₂ has only two dominant Raman peaks, the E¹2g, in-plane vibration at 381 cm-1, driven by the lateral oscillation of S atoms, and the A1g, out-of-plane mode at 408 cm-1.⁴ In thin / 2D samples, the A1g peak (linked to the out-of-plane S vibrations) is significantly weaker than it is in the bulk crystal due to many fewer vdW forces between the layers (Figure 1). This out-of-plane peak also displays a redshift (to lower wavenumber values) in the thinner samples (Figure 2).⁴ By taking a single crystal and repeatedly thinning it we can see the clear trend in these spectral changes produced by manual exfoliation (Table 1).

Tracking Structural Variations 

The Raman peaks of MoS₂ can reveal much more information than simply layer thickness. The shifting ratio of the out-of-plane A1g peak to the in-plane E¹2g peak can be used to study interlayer physics in these 2D crystal structures. For example, a Raman peak ratio analysis can reveal interfacial boundary conditions (Figure 4). In this sample, there is a stronger out-of-plane component to the lattice vibration along the crystal face boundaries. Given that there are no obvious peak shifts from differing layer thicknesses, the increased vdW forces at the boundaries may be due to another phenomena, such as a localized electronic charge accumulation in the boundary region.

Conclusion 

Even with a seemingly simple molecular structure such as MoS₂ there is a huge wealth of information that can be gleaned from Raman spectroscopic analysis. Layer thicknesses, interlayer forces, and in-plane strain can all be quickly analyzed based on the two MoS₂ peaks. Monitoring changes in these in-plane and out-of-plane vibrations for this 2D semiconductor allows a researcher to characterize numerous properties with a rapid, non-destructive analysis.

4. Waters Corporation: A New Method for Measuring Particulates in Protein Drug Formulations with Complex Excipients

• Application note
• Full PDF for download

Protein drugs need to be highly stable in order to increase product shelf life and inhibit protein aggregation which presents an immunogenic risk¹. To achieve protein drug stability, formulators use an array of water-soluble excipients including various buffers, detergents, sugars and other compounds to inhibit protein aggregate formation². 

Measuring the quality and the state of the excipients in a formulation is a big challenge. Each formulation parameter plays a key role in determining its stability, but due to the nature and sheer variety of excipients, these materials can often confound protein particle measurements³. This measurement gap is accentuated in flowbased subvisible particle analyzers, where the protein sample cannot be reanalyzed to gain greater insights of the formulation’s state. Running subsequent measurements enables formulators to gain greater insights on the state of the protein formulation’s components and its overall stability.

The HORIZON system, powered by backgrounded membrane imaging (BMI), enables users the unique ability to conduct serial wash measurements of protein formulations filtered on a membrane, to dissolve water soluble excipients and reveal the hidden insights of a formulation’s state. In this application note, we present three independent case studies that leverage the HORIZON system’s unique capability to analyze samples after serial washes to investigate the impact on the number of protein and excipient particulates in the sample to gain a clearer understanding of the formulation state.

Results and Discussion

Study 2 — Protein Aggregate Solubility and Adsorption to the Surface

In this case study we used IgG aggregates using the same sample preparation procedure described above and created two stock IgG solutions using PBS and DI water respectively. We ran 2X serial dilutions of the samples in their corresponding buffers from stock (1X) down to 32X dilutions. Samples were filtered through a HORIZON filter plate and subsequently measured using 50 µL of sample per well, measuring N = 4 samples per condition. For this experiment, the background of the software plate was cloned 3 times. All the wells were washed with 50 µL DI water, and remeasured, and this process was repeated 3 times for each wash step. 

Serial dilutions of IgG aggregates in both buffers showed linear counts drop behavior (R2 > 0.99), and very similar counts with stock IgG concentrations hovering close to 1E5 particles/mL for both stock conditions (Figure 4). After the first wash, both buffer types saw at most 20% of the counts drop for concentrated samples, potentially from the dissolution of soluble aggregates. Additional washing resulted in no counts increase or decrease within measurement error. 

Conclusion 

Serial membrane washing can help unveil critical details of a formulation. In the first two case studies, we explored how irreversible protein aggregates tend to be dense (dark in the image), amorphous, and do not disappear upon membrane washing as verified by visual microscopic membrane inspection and by counts analysis. Protein aggregates’ lack of solubility and their strong binding to the membrane surface allow one to count them reliably while uncovering the presence of other water-soluble excipients particles. This is important since the key objective of particle analysis in protein drug samples is to measure the insoluble protein aggregates since they tend to be immunogenic⁵. 

With protein aggregates being insoluble, this helped us deduce in the first case study that the faint, directional and water-soluble particles were salt crystals. Their presence also coincided with the age of the buffer (30 days), potentially pointing to time-related buffer degradation. The second case study confirmed the insolubility of the aggregates, with virtually no change in counts even after 3 serial washes. The third case study uncovered that protein solutions formulated in concentrated excipient conditions can show elevated counts. However, the excipient particle counts, arising from sucrose or polysorbate particles, could be washed away with a single wash to enable counting of the true protein aggregates. Also of interest in the third case study is that the IgG solution that was formulated without concentrated excipients showed significantly lower particle counts (nearly half) than those that were formulated in 10% sucrose and 0.05% polysorbate. This is a reminder that a higher excipient concentration does not necessarily result in higher formulation stability. The ability to get to the right formulation as quickly as possible requires one to obtain deep insights into all components of the formulation. The HORIZON system’s ability to clone original plate backgrounds to rapidly reanalyze the samples enables an unprecedented opportunity to learn more about the state of a proteindrug formulation. Key insights to your formulations are only a single 50 µL membrane wash away.