Protein drug stability: a formulation challenge

By S. Frokjaer, Daniel E. Otzen. Nature reviews. Drug discovery, 2005

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The CamSol method of rational design of protein mutants with enhanced solubility. (2015, background): “More generally, insufficient solubility represents a major bottleneck for the development of protein-based drugs, as protein aggregates not only are non-functional but also can be toxic and may elicit an immune response in the patient [14,28].”
Exploiting sequence and stability information for directing nanobody stability engineering (2017, background): “Its relevance becomes more and more apparent for therapeutic strategies, during which antibodies are usually administered at high concentrations [15,16].”
Hydrogels in controlled release formulations: network design and mathematical modeling. (2006, background): “Hydrogels offer an important “stealth” characteristic in vivo owing to their hydrophilicity which increases the in vivo circulation time of the delivery device by evading the host immune response and decreasing phagocytic activities [37,38].”
Protein therapeutics: a summary and pharmacological classification (2008, background): “The protein's stability, folding, and tendency to aggregate may be different in large-scale production and storage systems than in those used to produce the protein for animal testing and clinical trial”