GEN-MKT-18-7897-A
Feb 18, 2026 | Biopharma, Blogs, Pharma | 0 comments
Read time: 3 minutes
For decades, SCIEX has been part of bioanalytical innovation, empowering scientists in pharma and biopharma to push the boundaries of sensitivity, accuracy, and throughput. Across complex workflows and increasingly challenging therapeutic modalities.
Today, we’re spotlighting three peer‑reviewed publications, spanning nearly thirty years, that reflect how the scientific community continues to innovate. From oligonucleotide quantitation to protein bioanalysis, these studies highlight the evolution in the field and the long-term partnerships we value.
Publication: 🔗 https://pubs.acs.org/doi/full/10.1021/ac0618674
The study showcased how thoughtful chromatographic design, structured optimization, and careful attention to matrix effects could deliver reliable quantitation even in challenging biological samples. Many of the best practices introduced here, including instrument stability, ionization efficiency, and systematic validation, still underpin quantitative workflows today.
Abstract
Electrospray ionization (ESI) liquid chromatography−tandem mass spectrometry (LC/MS/MS) assays provide high-throughput and selective methods for quantitation of small molecules. Use of LC/MS/MS assays for macromolecules, like oligonucleotides, is challenging due to lack of sensitivity and low analyte recovery from biomatrixes. Due to this fact, the method of choice for oligonucleotides quantitation remains hybridization-based ligand-binding assays…
Publication: 🔗 https://pubs.acs.org/doi/full/10.1021/ac501837t
This publication introduced an innovative, cost-effective approach for protein depletion using combinations of organic solvents and acids, validated through signature peptide monitoring. The result? Cleaner extracts, improved sensitivity, and greater confidence in LC–MS/MS quantitation of therapeutic proteins.
We have developed an innovative method to remove albumin from plasma/serum samples for the LC-MS/MS quantitation of therapeutic proteins. Different combinations of organic solvents and acids were screened for their ability to remove albumin from plasma and serum samples. Removal efficiency was monitored by two signature peptides (QTALVELVK and LVNEVTEFAK) from albumin …
Publication: 🔗 https://www.tandfonline.com/doi/full/10.1080/…
This 2024 publication captures the cutting edge: hybridization‑based LC–MS/MS approach to measure trace levels of free antisense oligonucleotide payload in complex biological matrices. It demonstrates how advanced workflows, combining sample prep with sensitive mass spectrometry, are enabling scientists to tackle the challenges of next‑generation modalities.
We have developed an innovative method to remove albumin from plasma/serum samples for the LC-MS/MS quantitation of therapeutic proteins. Different combinations of organic solvents and acids were screened for their ability to remove albumin from plasma and serum samples. Removal efficiency was monitored by two signature peptides (QTALVELVK and LVNEVTEFAK) from albumin. Isopropanol with 1.0% trichloroacetic acid was found to be the most effective combination to remove albumin while retaining the protein of interest. Our approach was compared with a commercial albumin depletion kit on both efficiency of albumin removal and recovery of target proteins…
Each decade has brought new questions and new scientific ingenuity to the forefront. And through it all, SCIEX solutions and partnerships have helped researchers stay ahead of the curve.
As therapeutic innovation accelerates, bioanalysis will continue to evolve. Modalities will diversify. Performance expectations will rise. Workflows will become more hybrid, more integrated, and more data‑driven. SCIEX is committed to supporting scientists on that journey with tools designed not just for today’s challenges, but for tomorrow’s discoveries.
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As an analytical strategy, middle-down mass spectrometry (MS) workflows characterize biotherapeutic proteins by analyzing large, digested protein fragments or defined subunits, rather than fully intact proteins (top-down) or digested peptides (bottom-up). A middle-down strategy combines the strengths of top-down and bottom-up approaches by delivering high sequence coverage and structural specificity while maintaining relatively simple sample preparation. In practice, middle-down analysis enables accurate mass measurement, rapid sequence confirmation, and localization of key post-translational modifications (PTMs) on protein subunits that are directly relevant to product quality.
In biopharmaceutical development, sequence variants (SV) are considered an inherent risk of producing complex proteins in living systems. Sequence variants are unintended changes to the amino acid sequence of a biotherapeutic and can be caused by errors in transcription or translation in the host cell, or cell culture and process conditions. Detailed analysis of SVs is important in process and product development to ensure the drug’s safety and efficacy. Even low‑level sequence variants can have significant implications for product quality, safety, and efficacy, making their accurate detection and characterization a critical requirement across development, process optimization, and regulatory submission.
CE‑SDS remains a cornerstone assay for characterizing fragmentation, aggregation, and product‑related impurities in therapeutic proteins. UV detection has been the long‑standing standard. However, it frequently struggles with baseline noise, limited sensitivity for minor fragments, and subjective integration.
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