Výsledky vyhledávání - "Robert W. Payne"

Denaturation and Aggregation of Interferon-τ in Aqueous Solution

Autor: Charles S. Henry, Derrick S. Katayama, Gabriel J. Evans, Chelsey L. Gilley-Dunn, Ryan E. Holcomb, Nathan S. Krammes, Ryan R. Manning, Glenn A. Wilson, Mark C. Manning, Auria A. Tellechea, Nathaniel J. Zbacnik, Robert W. Payne, Ryan J. Krammes, Brian Murphy

Publikováno v: Pharmaceutical research. 35(7)

To evaluate the different degrees of residual structure in the unfolded state of interferon-τ using chemical denaturation as a function of temperature by both urea and guanidinium hydrochloride. Asymmetrical flow field-flow fractionation (AF4) using

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c12119cf83ca03c7e7399800386227fa
https://pubmed.ncbi.nlm.nih.gov/29744598

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Product development issues for PEGylated proteins

Autor: Mark C. Manning, Robert W. Payne, Brian Murphy

Publikováno v: Pharmaceutical Development and Technology. 16:423-440

Covalent attachment of poly(ethylene) glycol (PEG) groups to proteins, a process commonly called PEGylation, is often used to improve the performance of a protein in vivo. To date, at least eight such PEGylated peptide and protein conjugates have bee

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::539646e251dda5a47fe5ea56ab93339f
https://doi.org/10.3109/10837450.2010.513990

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Stability of Protein Pharmaceuticals: An Update

Autor: Brian Murphy, Robert W. Payne, Derrick S. Katayama, Mark C. Manning, Danny K. Chou

Publikováno v: Pharmaceutical Research. 27:544-575

In 1989, Manning, Patel, and Borchardt wrote a review of protein stability (Manning et al., Pharm. Res. 6:903-918, 1989), which has been widely referenced ever since. At the time, recombinant protein therapy was still in its infancy. This review summ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa66c12639944fbc397b06c36daab2fb
https://doi.org/10.1007/s11095-009-0045-6

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Stability of lyophilized teriparatide, PTH(1-34), after reconstitution

Autor: Glenn A. Wilson, Gene Merutka, Mark C. Manning, Brian Murphy, Charles S. Henry, James E. Matsuura, Robert W. Payne

Publikováno v: European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V. 99

The peptide teriparatide, also known as parathyroid hormone (1-34), PTH(1-34), was developed for intranasal delivery, requiring extended stability of the reconstituted product for up to four weeks at room temperature. Lyophilized formulations of PTH(

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98a9da4c1b3f3c7456dcf3138fad6c5d
https://pubmed.ncbi.nlm.nih.gov/26620825

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Second virial coefficient determination of a therapeutic peptide by self-interaction chromatography

Autor: Robert W. Payne, Charles S. Henry, Jie Di, David Heilman, Brian L. Bray, John Moschera, Mark C. Manning, Ralph Tarantino, Sam Del Terzo, Rajiv Nayar

Publikováno v: Biopolymers. 84:527-533

Self-interaction of macromolecules has been shown to play an important role in a number of physical processes, including crystallization, solubility, viscosity, and aggregation. Peptide self-interaction is not as well studied as for larger proteins,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef8a1a6024051bd00c56eeeef1e880ab
https://doi.org/10.1002/bip.20554

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Stability of lyophilized sucrose formulations of an IgG1: subvisible particle formation

Autor: Brian Murphy, Janice M. Davis, Mark C. Manning, Alan C. Herman, Ning Zhang, James E. Matsuura, Ahmad M. Abdul-Fattah, Robert W. Payne

Publikováno v: Pharmaceutical development and technology. 18(4)

Eight lyophilized formulations of a IgG1 monoclonal antibody (MAb) were prepared containing increasing levels of sucrose. In addition, three of the formulations had sorbitol added at a level of 5% w/w relative to sucrose. The samples were stored for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a7627f0e0d6a3dad7a6238fa8373241
https://pubmed.ncbi.nlm.nih.gov/22813478

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Structure, stability, and mobility of a lyophilized IgG1 monoclonal antibody as determined using second-derivative infrared spectroscopy

Autor: Ahmad M. Abdul-Fattah, Brian Murphy, Robert W. Payne, Janice M. Davis, Mark C. Manning, Alan C. Herman, James E. Matsuura, Ning Zhang

Publikováno v: Journal of pharmaceutical sciences. 101(1)

There are many aspects of stabilization of lyophilized proteins. Of these various factors, retention of native structure, having sufficient amount of stabilizer to embed the protein within an amorphous matrix, and dampening β-relaxations have been s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a1b3867951d813096d9cd51bc46a92b
https://pubmed.ncbi.nlm.nih.gov/21918984

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