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In this paper, a systematic approach is presented to develop a lyophilized high concentration protein formulation.
In protein formulation development, shaking stress is often employed to assess the physical stability of antibody formulations against aggregation.
In addition, we discussed the feasibility of implementing HDX-MS with these peptide probes in protein formulation development.
To stabilize a protein formulation different classes of excipients are used in combination after carefully selecting through laborious and time consuming trial and error experiments.
The described high-throughput methods are well suited for characterization of multiple protein formulation compositions with minimized resources such as time and material.
In this review several analytical challenges that may be encountered during protein formulation development of complex formulations are discussed through recent examples.
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Understanding these aspects is critical in the rational design of stable protein formulations.
In this study, microfluidic technology was employed to develop protein formulations.
The potential interrelationships between protein conformational and chemical stability are discussed in the context of designing stable protein formulations.
Surfactants, polysaccharides and salts are added to pharmaceutical products to stabilize protein formulations and to avoid denaturalization and aggregation [1, 5, 6].
A drawback of this innovative technology is that problems are encountered when processing high-concentrated amorphous materials, particularly protein formulations.
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