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Stabilization of proteins in solid form
Immunogenicity of aggregated or otherwise degraded protein delivered from depots or other biopharmaceutical products is an increasing concern, and the ability to deliver stable, active protein is of central importance. We review characterization approaches for solid protein dosage forms with respect...
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| Published in: | Advanced drug delivery reviews 2015-10, Vol.93, p.14-24 |
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| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c525t-5aae3719f2c648f41b861eaba357505fc57da352a350ebf104420c99faffb5e13 |
| container_end_page | 24 |
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| container_title | Advanced drug delivery reviews |
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| creator | Cicerone, Marcus T. Pikal, Michael J. Qian, Ken K. |
| description | Immunogenicity of aggregated or otherwise degraded protein delivered from depots or other biopharmaceutical products is an increasing concern, and the ability to deliver stable, active protein is of central importance. We review characterization approaches for solid protein dosage forms with respect to metrics that are intended to be predictive of protein stability against aggregation and other degradation processes. Each of these approaches is ultimately motivated by hypothetical connections between protein stability and the material property being measured. We critically evaluate correlations between these properties and stability outcomes, and use these evaluations to revise the currently standing hypotheses. Based on this we provide simple physical principles that are necessary (and possibly sufficient) for generating solid delivery vehicles with stable protein loads. Essentially, proteins should be strongly coupled (typically through H-bonds) to the bulk regions of a phase-homogeneous matrix with suppressed β relaxation. We also provide a framework for reliable characterization of solid protein forms with respect to stability.
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| doi_str_mv | 10.1016/j.addr.2015.05.006 |
| format | article |
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[Display omitted]</description><subject>Aggregation</subject><subject>Chemistry, Pharmaceutical - methods</subject><subject>Delayed-Action Preparations</subject><subject>Drug Delivery Systems</subject><subject>Drug Stability</subject><subject>Dynamic stabilization</subject><subject>Humans</subject><subject>Hydrobromic Acid</subject><subject>Lyophilization</subject><subject>Protein stability</subject><subject>Proteins - administration & dosage</subject><subject>Proteins - chemistry</subject><subject>Proteins - immunology</subject><subject>Water substitution</subject><issn>0169-409X</issn><issn>1872-8294</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><recordid>eNp9kE1LxDAQhoMo7vrxBzxIb3rpOkmbNgERRPwCwYMK3kKaTjRLt1mTrqC_3iyri16ECQnMM2-Gh5ADChMKtDqZTnTbhgkDyieQCqoNMqaiZrlgstwk4wTJvAT5PCI7MU4BKKsr2CYjxqVggooxOXoYdOM696kH5_vM22we_ICuj5nrs-g712bWh9ke2bK6i7j_fe-Sp6vLx4ub_O7--vbi_C43nPEh51pjUVNpmalKYUvaiIqibnTBaw7cGl636c3SAWwshbJkYKS02tqGIy12ydkqd75oZtga7IegOzUPbqbDh_Laqb-d3r2qF_-uyooVkssUcPwdEPzbAuOgZi4a7Drdo19ERWtWSyEKgISyFWqCjzGgXX9DQS0Nq6laGlZLwwpSQZWGDn8vuB75UZqA0xWASdO7w6CicdgbbF1AM6jWu__yvwCOZI0w</recordid><startdate>20151001</startdate><enddate>20151001</enddate><creator>Cicerone, Marcus T.</creator><creator>Pikal, Michael J.</creator><creator>Qian, Ken K.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-2718-6533</orcidid><orcidid>https://orcid.org/0000-0002-6850-1878</orcidid></search><sort><creationdate>20151001</creationdate><title>Stabilization of proteins in solid form</title><author>Cicerone, Marcus T. ; Pikal, Michael J. ; Qian, Ken K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c525t-5aae3719f2c648f41b861eaba357505fc57da352a350ebf104420c99faffb5e13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Aggregation</topic><topic>Chemistry, Pharmaceutical - methods</topic><topic>Delayed-Action Preparations</topic><topic>Drug Delivery Systems</topic><topic>Drug Stability</topic><topic>Dynamic stabilization</topic><topic>Humans</topic><topic>Hydrobromic Acid</topic><topic>Lyophilization</topic><topic>Protein stability</topic><topic>Proteins - administration & dosage</topic><topic>Proteins - chemistry</topic><topic>Proteins - immunology</topic><topic>Water substitution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cicerone, Marcus T.</creatorcontrib><creatorcontrib>Pikal, Michael J.</creatorcontrib><creatorcontrib>Qian, Ken K.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Advanced drug delivery reviews</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cicerone, Marcus T.</au><au>Pikal, Michael J.</au><au>Qian, Ken K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stabilization of proteins in solid form</atitle><jtitle>Advanced drug delivery reviews</jtitle><addtitle>Adv Drug Deliv Rev</addtitle><date>2015-10-01</date><risdate>2015</risdate><volume>93</volume><spage>14</spage><epage>24</epage><pages>14-24</pages><issn>0169-409X</issn><eissn>1872-8294</eissn><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-3</notes><notes>content type line 23</notes><notes>ObjectType-Review-1</notes><abstract>Immunogenicity of aggregated or otherwise degraded protein delivered from depots or other biopharmaceutical products is an increasing concern, and the ability to deliver stable, active protein is of central importance. We review characterization approaches for solid protein dosage forms with respect to metrics that are intended to be predictive of protein stability against aggregation and other degradation processes. Each of these approaches is ultimately motivated by hypothetical connections between protein stability and the material property being measured. We critically evaluate correlations between these properties and stability outcomes, and use these evaluations to revise the currently standing hypotheses. Based on this we provide simple physical principles that are necessary (and possibly sufficient) for generating solid delivery vehicles with stable protein loads. Essentially, proteins should be strongly coupled (typically through H-bonds) to the bulk regions of a phase-homogeneous matrix with suppressed β relaxation. We also provide a framework for reliable characterization of solid protein forms with respect to stability.
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| fulltext | fulltext |
| identifier | ISSN: 0169-409X |
| ispartof | Advanced drug delivery reviews, 2015-10, Vol.93, p.14-24 |
| issn | 0169-409X 1872-8294 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4623959 |
| source | ScienceDirect Freedom Collection |
| subjects | Aggregation Chemistry, Pharmaceutical - methods Delayed-Action Preparations Drug Delivery Systems Drug Stability Dynamic stabilization Humans Hydrobromic Acid Lyophilization Protein stability Proteins - administration & dosage Proteins - chemistry Proteins - immunology Water substitution |
| title | Stabilization of proteins in solid form |
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