The Osmolality and Hemolysis of High-Concentration Monoclonal Antibody Formulations.

Purposes: Highly concentrated monoclonal antibody (mAb) formulations for subcutaneous administration are becoming increasingly preferred within the biopharmaceutical industry for ease of use and improved patient compliance. A common phenomenon observed in the industry is that osmolality detected via freezing-point depression (FPD) in high-concentration mAb formulations is much higher than the theoretical concentrations, yet the occurrence of this phenomenon and its possible safety issues have been rarely reported.

Methods: The current study summarized theoretical osmolality of U.

Freeze-Dried Biopharmaceutical Formulations are Surprisingly Less Stable than Liquid Formulations during Dropping.

Purposes: This article describes an interesting phenomenon in which optimized freeze-dried (FD) biopharmaceutical formulations are generally more prone to degradation than their liquid counterparts during dropping and proposes an underlying cause for this surprising phenomenon.

Methods: Two monoclonal antibodies (mAbs) and a fusion protein (FP) were used as model biopharmaceuticals. The stability after dropping stress was determined by ultraviolet-visible (UV-Vis), size exclusion high-performance liquid chromatography (SE-HPLC), micro-flow imaging (MFI), and dynamic light scattering (DLS).

Copper-Catalyzed Remote C(sp)-H Amination of Carboxamides.

Here we report a method for the site-selective intermolecular C(sp)-H amination of carboxamides by merging transition-metal catalysis and the hydrogen atom transfer strategy. The reaction proceeds through a sequence of favorable single-electron transfer, 1,5-hydrogen atom transfer, and C-N cross-coupling steps, thus allowing access to a series of desired products. This reaction could accommodate a wide diversity of nitrogen nucleophiles as well as demonstrate excellent chemoselectivity and functional group compatibility.