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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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Pressure dependence of subtilisin crystallization kinetics

TL;DR: The effect of atmospheric to 100 MPa on crystallization of Purafect subtilisin was investigated in this article, where the overall crystallization rate was lower at high pressures and short exposures to high pressure followed by atmospheric crystallization did not increase the overall crystalization rate.
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Population balance modeling of aggregation kinetics of recombinant human interleukin-1 receptor antagonist.

TL;DR: The kinetics of benzyl alcohol-induced nonnative aggregation of recombinant human interleukin-1 receptor antagonist (rhIL-1ra) were investigated using a population balance model and the physical relevance of the information obtained from this model render it a useful tool to study protein aggregation kinetics and the effects of excipients on this process.
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Storage stability of keratinocyte growth factor-2 in lyophilized formulations: effects of formulation physical properties and protein fraction at the solid-air interface.

TL;DR: Lyophilized formulations of keratinocyte growth factor-2 (KGF-2) were prepared with a range of disaccharide (sucrose or trehalose) and hydroxyethyl starch (HES) mass ratios and degradation rates were highest in formulations wherein the protein's structure was most perturbed, and wherein β relaxations were fastest.
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Single-administration, thermostable human papillomavirus vaccines prepared with atomic layer deposition technology.

TL;DR: New technologies to prepare thermostable, single-shot, prime-boost microparticle vaccines may overcome current limitations in HPV vaccine delivery as well as being widely applicable to other antigens.
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Contributions of local mobility and degree of retention of native secondary structure to the stability of recombinant human growth hormone (rhGH) in glassy lyophilized formulations

TL;DR: Recombinant human growth hormone was used as a model in lyophilized formulations to investigate how protein degradation pathways of aggregation, deamidation and oxidation are linked to glassy state dynamics and the structure of protein immobilized in glassy matrices.