Abstract In 1989, Manning, Patel, and Borchardt wrote a review of protein stability (Manning
et al., Pharm. Res. 6: 903–918, 1989), which has been widely referenced ever since. At the …

Develo** recombinant protein pharmaceuticals has proved to be very challenging
because of both the complexity of protein production and purification, and the limited …

One of the most challenging tasks in the development of protein pharmaceuticals is to deal
with physical and chemical instabilities of proteins. Protein instability is one of the major …

Control and analysis of protein aggregation is an increasing challenge to pharmaceutical
research and development. Due to the nature of protein interactions, protein aggregation …

Histidine (His) carries a unique heteroaromatic imidazole side chain and plays irreplaceable
functional roles in peptides and proteins. Existing strategies for site-selective histidine …

Solid-state is the preferred choice for storage of protein therapeutics to improve stability and
preserve the biological activity by decreasing the physical and chemical degradation …

Protein aggregation in biotherapeutics has been identified to increase immunogenicity,
leading to immune-mediated adverse effects, such as severe allergic responses including …

Maintaining the structure of protein and peptide drugs has become one of the most important
goals of scientists in recent decades. Cold and thermal denaturation conditions …

The solid state is preferred for many proteins due to their marginal stability in solution.
However, even in the solid state, chemical and physical degradation can occur on the time …

Buffers comprise an integral component of protein formulations. Not only do they function to
regulate shifts in pH, they also can stabilize proteins by a variety of mechanisms. The ability …