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Conjugation of monoclonal antibodies to super paramagnetic nanoparticles is an effective method for cancer diagnosis and treatment. In this study the humanized anti her2/neu monoclonal antibody- Herceptin- was conjugated to super paramagnetic iron oxide (SPIO) nanoparticles using EDC method. The concentration of the conjugated antibodies was measured by Bradford assay. The antibody-nanoparticle conjugates were incubated with SKBR-3 and T47D human breast carcinoma cell lines and the presence of the conjugates on cell surface was confirmed by Prussian blue iron staining method. Conjugation of Herceptin to SPIO resulted in a precipitate-free conjugate containing 20µg antibody/mg SPIO. Prussian blue iron-staining of cells showed successful binding of the conjugates to the cell surfaces. Conjugation of monoclonal antibodies to SPIO may be a useful method for detection of tumor cells, especially by MRI techniques.
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Adv Pharm Bull
July 2025
R.C. Patel Institute of Pharmaceutical Education and Research, Industrial Pharmacy Laboratory, Department of Pharmaceutics, Shirpur 425405, Maharashtra, India.
Treatment of glioblastoma multiforme (GBM) has been a great challenge before medical fraternity since last century owing to a median survival of less than 15 months, despite of intensive therapy. Neurosurgeries, intense chemotherapy, advanced radiotherapy, and targeted therapies have bought some extension to the life of GBM patients. Combination and targeted therapies could bring a concrete approach to tackle the complexities of GBM treatment.
View Article and Find Full Text PDFEJNMMI Radiopharm Chem
September 2025
Department of Public Health and Caring Sciences, Uppsala University, Uppsala, 751 85, Sweden.
Background: Alzheimer's disease (AD) is increasingly recognized as a multifactorial disorder with vascular contributions, including a pro-coagulant state marked by fibrin deposition in the brain. Fibrin accumulation may exacerbate cerebral hypoperfusion and neuroinflammation, leading to neurodegeneration. Identifying patients with this pathology could enable targeted anticoagulant therapy.
View Article and Find Full Text PDFOncol Res
September 2025
The Breast Center, Cancer Hospital of Shantou University Medical College, Guangdong Provincial Key Laboratory of Breast Cancer Diagnosis and Treatment, Shantou, 515031, China.
Background: Breast cancer remains a leading cause of morbidity and mortality among women worldwide, with significant geographic disparities in its impact. While human epidermal growth factor receptor 2 (HER2)-targeted therapies, such as trastuzumab, have improved outcomes for HER2-positive breast cancer, challenges like therapy resistance persist, highlighting the need for novel treatments. Recent developments in antibody-drug conjugates (ADCs), particularly disitamab vedotin (RC48), show promising efficacy in targeting both HER2-positive and HER2-low expression tumors, warranting further investigation through real-world studies to assess its broader clinical applicability.
View Article and Find Full Text PDFACS Omega
September 2025
Ajinomoto Bio-Pharma Services, 11040 Roselle Street, San Diego, California 92121, United States.
Antibody-drug conjugates (ADCs) represent a transformative class of cancer therapies that combine the specificity of monoclonal antibodies with the cytotoxicity of potent drug payloads. This study presents the development and evaluation of a novel linker platform designed to enhance ADC stability and pharmacokinetics by addressing the limitations associated with traditional cleavable linkers. Using trastuzumab conjugated with a payload linker consisting of this platform and exo-EVC-Exatecan (APL-1082), we examined key parameters, including efficacy and pharmacokinetic profiles in rat models, to directly compare it with the clinically validated trastuzumab-deruxtecan (T-DXd, Enhertu).
View Article and Find Full Text PDFAnal Chim Acta
November 2025
Guangdong Provincial Key Laboratory of Food Quality and Safety, South China Agricultural University, Guangzhou, 510642, China. Electronic address:
Egg yolk immunoglobulin (IgY) has emerged as a promising alternative to monoclonal antibodies (mAbs) due to its facile extraction, higher yield, and greater tolerance to organic solvents. This work developed a selective IgY antibody against bongkrekic acid (BA) and isobongkrekic acid (IsoBA), the lethal toxins produced by Burkholderia gladioli pv. Cocovenenans (BGC), which led to severe food poisoning incidents and resulted in casualties.
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