T
Theodore W. Randolph
Researcher at University of Colorado Boulder
Publications - 313
Citations - 22031
Theodore W. Randolph is an academic researcher from University of Colorado Boulder. The author has contributed to research in topics: Protein aggregation & Supercritical fluid. The author has an hindex of 77, co-authored 306 publications receiving 20474 citations. Previous affiliations of Theodore W. Randolph include MedImmune & University of Colorado Denver.
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Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation
TL;DR: The purpose of the current review is to provide a fundamental understanding of the mechanisms by which proteins aggregate and by which varying solution conditions, such as temperature, pH, salt type, salt concentration, cosolutes, preservatives, and surfactants, affect this process.
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Rational design of stable lyophilized protein formulations: some practical advice.
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Water-in-carbon dioxide microemulsions : an environment for hydrophiles including proteins
Keith P. Johnston,Kristi L. Harrison,Matthew J. Clarke,Steven M. Howdle,Mark P. Heitz,Frank V. Bright,Claude Carlier,Theodore W. Randolph +7 more
TL;DR: In this article, the protein bovine serum albumin (BSA) with a molecular weight of 67,000 is soluble in a carbon dioxide-continuous phase with a nontoxic ammonium carboxylate perfluoropolyether surfactant.
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Overlooking subvisible particles in therapeutic protein products: Gaps that may compromise product quality
John F. Carpenter,Theodore W. Randolph,Wim Jiskoot,Daan J.A. Crommelin,C. Russell Middaugh,Gerhard Winter,Ying-Xin Fan,Susan L. Kirshner,Daniela Verthelyi,Steven Kozlowski,Kathleen A. Clouse,Patrick G. Swann,Amy S. Rosenberg,Barry Cherney +13 more
TL;DR: The purpose of this commentary is to provide brief summaries on the factors affecting protein aggregation and the key aspects of protein aggregation that are associated with immunogenicity, and emphasize the current scientific gaps in understanding and analytical limitations for quantitation of species of large protein aggregates that are referred to as subvisible particles.
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Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding.
TL;DR: Results show that hydrogen bonding between carbohydrate and protein is necessary to prevent dehydration-induced protein damage, however, hydrogen bonding alone is not sufficient to protect proteins during lyophilization in the absence of adequate freezing protection.