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Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering
In order to increase shelf life and minimize aggregation during storage, many biotherapeutic drugs are formulated and stored as either frozen solutions or lyophilized powders. However, characterizing amorphous solids can be challenging with the commonly available set of biophysical measurements used...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Research Network of Computational and Structural Biotechnology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5257034/ https://www.ncbi.nlm.nih.gov/pubmed/28138368 http://dx.doi.org/10.1016/j.csbj.2016.12.004 |
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author | Castellanos, Maria Monica McAuley, Arnold Curtis, Joseph E. |
author_facet | Castellanos, Maria Monica McAuley, Arnold Curtis, Joseph E. |
author_sort | Castellanos, Maria Monica |
collection | PubMed |
description | In order to increase shelf life and minimize aggregation during storage, many biotherapeutic drugs are formulated and stored as either frozen solutions or lyophilized powders. However, characterizing amorphous solids can be challenging with the commonly available set of biophysical measurements used for proteins in liquid solutions. Therefore, some questions remain regarding the structure of the active pharmaceutical ingredient during freezing and drying of the drug product and the molecular role of excipients. Neutron scattering is a powerful technique to study structure and dynamics of a variety of systems in both solid and liquid phases. Moreover, neutron scattering experiments can generally be correlated with theory and molecular simulations to analyze experimental data. In this article, we focus on the use of neutron techniques to address problems of biotechnological interest. We describe the use of small-angle neutron scattering to study the solution structure of biological molecules and the packing arrangement in amorphous phases, that is, frozen glasses and freeze-dried protein powders. In addition, we discuss the use of neutron spectroscopy to measure the dynamics of glassy systems at different time and length scales. Overall, we expect that the present article will guide and prompt the use of neutron scattering to provide unique insights on many of the outstanding questions in biotechnology. |
format | Online Article Text |
id | pubmed-5257034 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Research Network of Computational and Structural Biotechnology |
record_format | MEDLINE/PubMed |
spelling | pubmed-52570342017-01-30 Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering Castellanos, Maria Monica McAuley, Arnold Curtis, Joseph E. Comput Struct Biotechnol J Mini Review In order to increase shelf life and minimize aggregation during storage, many biotherapeutic drugs are formulated and stored as either frozen solutions or lyophilized powders. However, characterizing amorphous solids can be challenging with the commonly available set of biophysical measurements used for proteins in liquid solutions. Therefore, some questions remain regarding the structure of the active pharmaceutical ingredient during freezing and drying of the drug product and the molecular role of excipients. Neutron scattering is a powerful technique to study structure and dynamics of a variety of systems in both solid and liquid phases. Moreover, neutron scattering experiments can generally be correlated with theory and molecular simulations to analyze experimental data. In this article, we focus on the use of neutron techniques to address problems of biotechnological interest. We describe the use of small-angle neutron scattering to study the solution structure of biological molecules and the packing arrangement in amorphous phases, that is, frozen glasses and freeze-dried protein powders. In addition, we discuss the use of neutron spectroscopy to measure the dynamics of glassy systems at different time and length scales. Overall, we expect that the present article will guide and prompt the use of neutron scattering to provide unique insights on many of the outstanding questions in biotechnology. Research Network of Computational and Structural Biotechnology 2016-12-21 /pmc/articles/PMC5257034/ /pubmed/28138368 http://dx.doi.org/10.1016/j.csbj.2016.12.004 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Mini Review Castellanos, Maria Monica McAuley, Arnold Curtis, Joseph E. Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering |
title | Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering |
title_full | Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering |
title_fullStr | Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering |
title_full_unstemmed | Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering |
title_short | Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering |
title_sort | investigating structure and dynamics of proteins in amorphous phases using neutron scattering |
topic | Mini Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5257034/ https://www.ncbi.nlm.nih.gov/pubmed/28138368 http://dx.doi.org/10.1016/j.csbj.2016.12.004 |
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