Modification of biopharmaceutical molecules by covalent conjugation of polyethylene glycol
(PEG) molecules is known to enhance pharmacologic and pharmaceutical properties of …

All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

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 …

Abstract Treatment with therapeutic proteins is an attractive approach to targeting a number
of challenging diseases. Unfortunately, the native proteins themselves are often unstable in …

Over the past few decades, the complexity of molecular entities being advanced for
therapeutic purposes has continued to evolve. A main propellent fueling innovation is the …

Glycosylation is among the most common post-translational modifications that proteins
undergo that may affect many of their activities. It may also modify the underlying energy …

Highlights•Chemoselective reactions enable site-specific PEGylation.•PEG-based
conformational stabilization provides enhanced proteolytic resistance.•PEG-based protein …

For more than 40 years, protein–polymer conjugates have been widely used for many
applications, industrially and biomedically. These bioconjugates have been shown to …

It is well recognized that protein product development is far more challenging than that for
small‐molecule drugs. The major challenges include inherent sensitivity to different types of …

The drying of biomolecules into powdered formulations has become the main form of long-
term product stabilisation, allowing for the delivery of safe and efficient medicines. Stability of …