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- W2039741197 abstract "Early development of protein biotherapeutics using recombinant DNA technology involved progress in the areas of cloning, screening, expression and recovery/purification. As the biotechnology industry matured, resulting in marketed products, a greater emphasis was placed on development of formulations and delivery systems requiring a better understanding of the chemical and physical properties of newly developed protein drugs. Biophysical techniques such as analytical ultracentrifugation, dynamic and static light scattering, and circular dichroism were used to study protein–protein interactions during various stages of development of protein therapeutics. These studies included investigation of protein self-association in many of the early development projects including analysis of highly glycosylated proteins expressed in mammalian CHO cell cultures. Assessment of protein–protein interactions during development of an IgG1 monoclonal antibody that binds to IgE were important in understanding the pharmacokinetics and dosing for this important biotherapeutic used to treat severe allergic IgE-mediated asthma. These studies were extended to the investigation of monoclonal antibody–antigen interactions in human serum using the fluorescent detection system of the analytical ultracentrifuge. Analysis by sedimentation velocity analytical ultracentrifugation was also used to investigate competitive binding to monoclonal antibody targets. Recent development of high concentration protein formulations for subcutaneous administration of therapeutics posed challenges, which resulted in the use of dynamic and static light scattering, and preparative analytical ultracentrifugation to understand the self-association and rheological properties of concentrated monoclonal antibody solutions." @default.
- W2039741197 created "2016-06-24" @default.
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- W2039741197 date "2013-03-14" @default.
- W2039741197 modified "2023-10-10" @default.
- W2039741197 title "Assessment and significance of protein–protein interactions during development of protein biopharmaceuticals" @default.
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- W2039741197 doi "https://doi.org/10.1007/s12551-013-0109-z" @default.
- W2039741197 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5418437" @default.
- W2039741197 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28510158" @default.
- W2039741197 hasPublicationYear "2013" @default.