Solution behavior of a novel type 1 interferon, interferon-τ

Katayama, Derrick S.; Nayar, Rajiv; Chou, Danny K.; Campos, Jackie; Cooper, Julianne; Velde, David G. Vander; Villarete, Lorelie; Liu, C.P.; Manning, Mark C.

doi:10.1002/jps.20461

Cited by 28 publications

(21 citation statements)

References 30 publications

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“…Since pH 7 appears to produce a nativelike structure,23 three different buffers, Tris, phosphate, and histidine, capable of maintaining the pH of the solution at 7, were evaluated. Initial studies indicated that the thermal stability of the protein does vary significantly as a function of buffer species (vide infra).…”

Section: Resultsmentioning

confidence: 99%

“…Therefore, a detailed comparison was begun, where the buffer concentration was fixed at 20 mM and the salt concentration held constant at 100 mM. These conditions of pH 7, 20 mM buffer, and 100 mM sodium chloride were selected based on preformulation studies that showed the chemical stability and antiviral activity of IFN‐tau were optimal under these conditions 23…”

Section: Resultsmentioning

confidence: 99%

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Effect of buffer species on the thermally induced aggregation of interferon-tau

Katayama

Nayar

Chou

et al. 2006

Journal of Pharmaceutical Sciences

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Effect of buffer species on the thermally induced aggregation of interferon-tau

Katayama

Nayar

Chou

et al. 2006

Journal of Pharmaceutical Sciences

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“…Dilution was required because saturation was observed in undiluted samples containing aggregates; spectra were recorded immediately after dilution. Increased UV absorbance at 350 nm has been associated with the presence of IgG aggregates in solution, and an “aggregation index” based on UV absorbance has been reported 13, 14 . Here, the aggregation index (A.I.)…”

Section: Methodsmentioning

confidence: 99%

“…was determined in triplicate from the UV spectra using the equation A.I. = OD 350 /(OD 280 -OD 350 )×100, as reported by Katayama et al 13 .…”

Section: Methodsmentioning

confidence: 99%

Protein G, Protein A and Protein A-Derived Peptides Inhibit the Agitation Induced Aggregation of IgG

Zhang

Topp

2012

Mol. Pharmaceutics

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Controlling and preventing aggregation is critical to the development of safe and effective antibody drug products. The studies presented here test the hypothesis that Protein A and Protein G inhibit the agitation-induced aggregation of IgG. The hypothesis is motivated by the enhanced conformational stability of proteins upon ligand binding and the specific binding affinity of Protein A and Protein G to the Fc region of IgG. The aggregation of mixed human IgG from pooled human plasma was induced by agitation alone or in the presence of: (i) Protein A, (ii) Protein G or (iii) a library of 24 peptides derived from the IgG-binding domain of Protein A. Aggregation was assessed by UV spectroscopy, SDS-PAGE, high performance size-exclusion chromatography (HP-SEC), dynamic light scattering (DLS) and fluorescence spectroscopy. Additional information on IgG-ligand interactions was obtained using differential scanning fluorimetry (DSF) and competitive binding studies. The results demonstrate that Protein A provides near-complete inhibition of agitation-induced aggregation, while Protein G and two peptides from the peptide library show partial inhibition. The findings indicate that the IgG Protein A binding site is involved in the agitation-induced aggregation of IgG, and suggest a dominant role of colloidal interactions.

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“…A.I. was calculated using optical densities at 280 nm and 350 nm according to the method described by Katayama et al (2005) as follows:

normalA . normalI . = \frac{{OD}_{350}}{OD 280 - {OD}_{350}} \times 100

…”

Section: Methodsmentioning

confidence: 99%

Protein aggregation and lyophilization: Protein structural descriptors as predictors of aggregation propensity

Roughton

Iyer

Bertelsen

et al. 2013

Computers & Chemical Engineering

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Lyophilization can induce aggregation in therapeutic proteins, but the relative importance of protein structure, formulation and processing conditions are poorly understood. To evaluate the contribution of protein structure to lyophilization-induced aggregation, fifteen proteins were co-lyophilized with each of five excipients. Extent of aggregation following lyophilization, measured using size-exclusion chromatography, was correlated with computational and biophysical protein structural descriptors via multiple linear regression. Descriptor selection was performed using exhaustive search and forward selection. The results demonstrate that, for a given excipient, extent of aggregation is highly correlated by eight to twelve structural descriptors. Leave-one-out cross validation showed that the correlations were able to successfully predict the aggregation for a protein “left out” of the data set. Selected descriptors varied with excipient, indicating both protein structure and excipient type contribute to lyophilization-induced aggregation. The results show some descriptors used to predict protein aggregation in solution are useful in predicting lyophilized protein aggregation.

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Solution behavior of a novel type 1 interferon, interferon-τ

Cited by 28 publications

References 30 publications

Effect of buffer species on the thermally induced aggregation of interferon-tau

Effect of buffer species on the thermally induced aggregation of interferon-tau

Protein G, Protein A and Protein A-Derived Peptides Inhibit the Agitation Induced Aggregation of IgG

Protein aggregation and lyophilization: Protein structural descriptors as predictors of aggregation propensity

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