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Antivenom therapy is a critical intervention for treating the more than 5.000.000 envenomation accidents that occur each year around the world. These immunotherapeutic drugs are mostly produced following techniques developed more than fifty years ago with minor changes. Aggregate content has been described as one of the main causes of early adverse effects after intravenous administration of antivenoms. In this work we propose the introduction of a final polishing step to traditional antivenom manufacturing processes aimed at lowering the aggregate content in the final product. The refinement step proposed in this work is based on the selective capture of immunoglobulin aggregates by a cation exchange monolithic stationary phase. We show that this media can effectively remove aggregates in the final product under isotonic ion-strength and mildly acidic conditions following a negative chromatography strategy, thus making it a useful technique for producing higher quality products.
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http://dx.doi.org/10.1016/j.jchromb.2023.123978 | DOI Listing |
Mikrochim Acta
September 2025
Department of Surgical Oncology, Shaanxi Provincial People's Hospital, 256 Friendship West Road, Beilin District, Xi'an, 710068, Shaanxi, China.
Mycoplasma pneumonia, a primary aetiological agent of atypical pneumonia, necessitates the implementation of rapid point-of-care diagnostics. Lateral flow immunoassays (LFIAs) hold promise for point-of-care testing (POCT), yet their sensitivity levels are frequently constrained by probe affinity and matrix interference. We introduce an orientational labelling strategy that employs magnetic nanoparticles (MNPs) functionalized with staphylococcal protein A (SPA) to simultaneously enhance antibody orientation and facilitate magnetic enrichment.
View Article and Find Full Text PDFPLoS One
September 2025
Department of Chemistry, University of California, Irvine, California, United States of America.
Anti-Aβ antibodies are important tools for identifying structural features of aggregates of the Aβ peptide and are used in many aspects of Alzheimer's disease (AD) research. Our laboratory recently reported the generation of a polyclonal antibody, pAb2AT-L, that is moderately selective for oligomeric Aβ over monomeric and fibrillar Aβ and recognizes the diffuse peripheries of Aβ plaques in AD brain tissue but does not recognize the dense fibrillar plaque cores. This antibody was generated against 2AT-L, a structurally defined Aβ oligomer mimic composed of three Aβ-derived β-hairpins arranged in a triangular fashion and covalently stabilized with three disulfide bonds.
View Article and Find Full Text PDFJ Mol Recognit
September 2025
Protein Interactome Lab for Structural and Functional Biology, Advanced Centre for Treatment Research and Education in Cancer, Navi Mumbai, Maharashtra, India.
Systemic light-chain amyloidosis (AL) is caused by the misfolding and aggregation of immunoglobulin light chains (LCs), which natively form homodimers comprising variable (VL) and constant (CL) domains in each monomer. High sequence variability, particularly within the VL domain, results in varied structural changes and aggregation propensities, making it challenging to develop broadly effective native protein stabilizers/aggregation inhibitors, as each AL patient carries a unique light chain. Using artificial intelligence (AI)-based AlphaFold2, known for its accuracy in modeling folded proteins, we generated an extensive repertoire of structural models of full-length LCs from four amyloidogenic germlines: IGLV1(λ1), IGLV3(λ3), IGLV6(λ6), and IGKV1(κ1), over-represented in AL patients to identify germline-specific structural features.
View Article and Find Full Text PDFMAbs
December 2025
Antibody Discovery & Protein Engineering, Merck Healthcare KGaA, Darmstadt, Germany.
The discovery and development of multispecific antibodies present unique challenges in optimizing their physicochemical properties to enhance developability and manufacturability. Common developability challenges include increased risk of aggregation, high viscosity, poor solubility, low expression yields, complex purification requirements, greater propensity for fragmentation, immunogenicity, or pharmacokinetics. In this study, we systematically investigate the solution behavior of engineered bispecific IgG1-VHH constructs derived from a parental NKp30 ×EGFR natural killer cell engager (NKCE) molecule, focusing on colloidal stability, hydrophobicity, thermal stability, pH sensitivity, and viscosity.
View Article and Find Full Text PDFBiosensors (Basel)
August 2025
Biomedical Engineering Programme, School of Medicine, The Chinese University of Hong Kong, Shenzhen 518172, China.
Exosomes are membranous vesicles that play a crucial role as intercellular messengers. Cells secrete exosomes, which can be found in a variety of bodily fluids such as amniotic fluid, semen, breast milk, tears, saliva, urine, blood, bile, ascites, and cerebrospinal fluid. Exosomes have a distinct bilipid protein structure and can be as small as 30-150 nm in diameter.
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