Publications by authors named "E R Zartler"
Article Synopsis
- PF-06439535 (Zirabev) is a biosimilar of bevacizumab, and researchers evaluated its stability and functional activity after dilution for intravenous infusion under various storage conditions.
- The study involved diluting PF-06439535, storing it under specific temperatures, and testing its physicochemical and biological stability using several analytical techniques.
- Results showed no significant changes in protein concentration, visual characteristics, molecular weight variants, and charge variants over a 6-week period, indicating good stability of the drug product.
Introduction: The stability and functional activity of the trastuzumab biosimilar PF-05280014 (trastuzumab-qyyp; Trazimera), was assessed under extended in-use conditions.
Methods: PF-05280014 was diluted in 0.9% sodium chloride to final concentrations of 0.
The human gamma-herpesviruses Epstein-Barr virus (EBV) (HHV-4) and Kaposi's sarcoma-associated herpesvirus (KSHV) (HHV-8) are responsible for a number of diseases, including various types of cancer. Epstein-Barr nuclear antigen 1 (EBNA1) from EBV and latency-associated nuclear antigen (LANA) from KSHV are viral-encoded DNA-binding proteins that are essential for the replication and maintenance of their respective viral genomes during latent, oncogenic infection. As such, EBNA1 and LANA are attractive targets for the development of small-molecule inhibitors.
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- Epstein-Barr virus (EBV) is linked to 1-2% of human cancers, such as various lymphomas and gastric carcinoma, due to its persistent latent infection promoting tumor growth.
- EBNA1, a viral protein present in all EBV-related tumors, is crucial for viral functions and presents a target for developing treatments.
- Researchers have identified specific inhibitors that block EBNA1's DNA binding activity, showing effectiveness in lab models by suppressing tumor growth and altering important signaling pathways in nasopharyngeal carcinoma.
The increased interest in using monoclonal antibodies (mAbs) as a platform for biopharmaceuticals has led to the need for new analytical techniques that can precisely assess physicochemical properties of these large and very complex drugs for the purpose of correctly identifying quality attributes (QA). One QA, higher order structure (HOS), is unique to biopharmaceuticals and essential for establishing consistency in biopharmaceutical manufacturing, detecting process-related variations from manufacturing changes and establishing comparability between biologic products. To address this measurement challenge, two-dimensional nuclear magnetic resonance spectroscopy (2D-NMR) methods were introduced that allow for the precise atomic-level comparison of the HOS between two proteins, including mAbs.
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