Theodore W. Randolph

TL;DR: The purpose of the current review is to provide a fundamental understanding of the mechanisms by which proteins aggregate and by which varying solution conditions, such as temperature, pH, salt type, salt concentration, cosolutes, preservatives, and surfactants, affect this process.

TL;DR: In this article, the protein bovine serum albumin (BSA) with a molecular weight of 67,000 is soluble in a carbon dioxide-continuous phase with a nontoxic ammonium carboxylate perfluoropolyether surfactant.

TL;DR: The purpose of this commentary is to provide brief summaries on the factors affecting protein aggregation and the key aspects of protein aggregation that are associated with immunogenicity, and emphasize the current scientific gaps in understanding and analytical limitations for quantitation of species of large protein aggregates that are referred to as subvisible particles.

TL;DR: Results show that hydrogen bonding between carbohydrate and protein is necessary to prevent dehydration-induced protein damage, however, hydrogen bonding alone is not sufficient to protect proteins during lyophilization in the absence of adequate freezing protection.