Protein formulation and fill-finish operations

Stability of Protein Pharmaceuticals: An Update

“…One of the greatest challenges to the investigation of the causes of protein aggregation is that there is no single pathway by which proteins can form an aggregate (Table IV). Aggregation can have many causes, such as incorrect folding during protein expression, and perturbation of the native conformation during protein purification, formulation, freeze-thawing, freeze-drying, ultrafiltration/diafiltration, vial and syringe filling, pumping, transportation or storage (302)(303)(304)(305)(306). These processes can jeopardize product stability by exposing proteins to potentially damaging conditions, such as freezing, dehydration, extreme pH, air-liquid interfaces, solid-liquid interfaces, or high or low temperatures.…”

Physical and biophysical effects of polysorbate 20 and 80 on darbepoetin alfa

“…Surface-active agents, or surfactants, are often added to protein solutions to prevent physical damage or loss as mentioned. [5][6][7][8][9][10][11][12] Human serum albumin (HSA) has been used in a number of protein formulations as a stabilizer to prevent surface adsorption, especially at low protein concentrations. Recent concerns about the presence of infectious agents (e.g., viruses and prions) in mammalian products have prompted many regulatory agencies to prohibit the use of HSA and other similar additives, forcing the exploration of other options.…”

Unexpected improvement in stability and utility of cytochrome c by solution in biocompatible ionic liquids

“…Protection against degradation reactions may also enable new methodologies in cell biopreservation and protein purification (Patro et al, 2002). In this paper we investigate that long-term stability of a model protein when dissolved in a biocompatible ionic liquid and demonstrate retention of structure and activity.…”