Proteoglycans are a major family of glycoconjugates which participate in and regulate several cellular events and biological functions. Their glycan chains determine their physicochemical and biological properties. Capillary electrophoresis, because of its high resolving power and sensitivity, has been successfully used for the analysis of carbohydrates. The monosaccharide constituents, the disaccharide sulfation pattern, and the uronic acid distribution within glycan chains of proteoglycans determine their interactions with matrix effectors and are responsible for numerous effects. Determination of the chemical composition and identification of key structural components and domains of glycans are, therefore, essential in understanding the biological functions of proteoglycans. In this report an overview of the capillary electrophoresis methods used to analyze and characterize the structure of the glycan chains of proteoglycans is presented.
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http://dx.doi.org/10.1007/s002160100968 | DOI Listing |
Electrophoresis
January 2025
Department of Toxicology, Advanced Medical and Dental Institute, Universiti Sains Malaysia, Bertam, Kepala Batas, Pulau Pinang, Malaysia.
Advancements in food technology have increased the need for thorough analysis to ensure food safety, quality, and compliance with regulatory requirements. Capillary electrophoresis-mass spectrometry (CE-MS) has emerged as a powerful tool in food analysis due to its high separation efficiency, low sample consumption, and ability to handle complex matrices. However, challenges such as the use of volatile running buffers and maintaining the stability of the electrical circuit connecting the CE and MS systems have been addressed through advancements in interface designs, such as sheathless systems and optimized sheath-liquid compositions.
View Article and Find Full Text PDFElectrophoresis
January 2025
Pfizer, Analytical Research and Development, Chesterfield, Missouri, USA.
A significant limitation of imaged capillary electric focusing (icIEF) is the inability to identify and characterize specific species in the electropherogram. This has led to the development of complementary ion-exchange chromatography (IEX)-based methods that are amenable to either fraction collection and subsequent characterization or online IEX coupled to mass spectrometry. To overcome this limitation while maintaining the use of icIEF, novel approaches, including an icIEF separation and fractionation technology (MauriceFlex, ProteinSimple), have been developed.
View Article and Find Full Text PDFAnalyst
January 2025
Department of Chemistry & Biochemistry, New Mexico State University, Las Cruces, NM, 88003-001, USA.
Hydrodynamic radius () is a descriptive metric of protein structure with the potential to impact drug development, disease diagnosis, and other important research areas of molecular biology. Common instrumental methods for molecular size characterization are disadvantageous due to high sample consumption, measurements made in non-physiological conditions, and/or inaccurate size determinations. Capillary Taylor dispersion analysis (TDA) is a molecular sizing method that utilizes nL sample volumes and achieves absolute size determination without calibration or comparison to standards.
View Article and Find Full Text PDFForensic Sci Int Genet
January 2025
NimaGen BV, Hogelandseweg 88, Nijmegen 6545 AB, the Netherlands.
Forensic science takes advantage of population variability in autosomal Short Tandem Repeat (STR) lengths to establish human identification. The most common method for DNA profiling by STR is based on PCR, where the highly polymorphic STR regions are amplified and analysed using Capillary Electrophoresis (CE) or Massively Parallel Sequencing (MPS). MPS determines not only the repeat length, but also the repeat structure and variations in the flanking regions, making this method superior in discriminatory power compared to CE.
View Article and Find Full Text PDFTalanta
January 2025
Translational Glycomics Research Group, Research Institute of Biomolecular and Chemical Engineering, University of Pannonia, Veszprem, Hungary; Horváth Csaba Memorial Laboratory of Bioseparation Sciences, Research Center for Molecular Medicine, Faculty of Medicine, University of Debrecen, Hungary. Electronic address:
Sodium dodecyl sulfate capillary gel electrophoresis (SDS-CGE) is a frequently used analytical technique in size-based separation of proteins, playing a vital role in the biopharmaceutical industry for the analysis and characterization of therapeutic proteins, employing both UV and fluorescent detection. Understanding the effect of the operational parameters using easily applicable in migratio fluorescent labeling is increasingly critical, especially because multicapillary electrophoresis systems with fluorescent detection have recently gained prominence in high-throughput biopolymer analysis. In this study, the effects of the three most important user-adjustable operational parameters (temperature, gel concentration, and electric field strength) were investigated on the electrophoretic mobility and resolution of SDS-protein complexes in the presence of propidium iodide in the gel-buffer system.
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