High throughput screening of protein formulation stability: Practical considerations
The formulation of protein drugs is a difficult and time-consuming process, mainly due to the complexity of protein structure and the very specific physical and chemical properties involved. Understanding protein degradation pathways is essential for the success of a biopharmaceutical drug. The pres...
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| Veröffentlicht in: | European journal of pharmaceutics and biopharmaceutics 2007-02, Vol.65 (2), p.131-148 |
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| container_title | European journal of pharmaceutics and biopharmaceutics |
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| creator | Capelle, Martinus A.H. Gurny, Robert Arvinte, Tudor |
| description | The formulation of protein drugs is a difficult and time-consuming process, mainly due to the complexity of protein structure and the very specific physical and chemical properties involved. Understanding protein degradation pathways is essential for the success of a biopharmaceutical drug. The present review concerns the application of high throughput screening techniques in protein formulation development. A protein high throughput formulation (HTF) platform is based on the use of microplates. Basically, the HTF platform consists of two parts: (i) sample preparation and (ii) sample analysis. Sample preparation involves automated systems for dispensing the drug and the formulation ingredients in both liquid and powder form. The sample analysis involves specific methods developed for each protein to investigate physical and chemical properties of the formulations in microplates. Examples are presented of the use of protein intrinsic fluorescence for the analysis of protein aqueous properties (e.g., conformation and aggregation). Different techniques suitable for HTF analysis are discussed and some of the issues concerning implementation are presented with reference to the use of microplates. |
| doi_str_mv | 10.1016/j.ejpb.2006.09.009 |
| format | Article |
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Understanding protein degradation pathways is essential for the success of a biopharmaceutical drug. The present review concerns the application of high throughput screening techniques in protein formulation development. A protein high throughput formulation (HTF) platform is based on the use of microplates. Basically, the HTF platform consists of two parts: (i) sample preparation and (ii) sample analysis. Sample preparation involves automated systems for dispensing the drug and the formulation ingredients in both liquid and powder form. The sample analysis involves specific methods developed for each protein to investigate physical and chemical properties of the formulations in microplates. Examples are presented of the use of protein intrinsic fluorescence for the analysis of protein aqueous properties (e.g., conformation and aggregation). 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Understanding protein degradation pathways is essential for the success of a biopharmaceutical drug. The present review concerns the application of high throughput screening techniques in protein formulation development. A protein high throughput formulation (HTF) platform is based on the use of microplates. Basically, the HTF platform consists of two parts: (i) sample preparation and (ii) sample analysis. Sample preparation involves automated systems for dispensing the drug and the formulation ingredients in both liquid and powder form. The sample analysis involves specific methods developed for each protein to investigate physical and chemical properties of the formulations in microplates. Examples are presented of the use of protein intrinsic fluorescence for the analysis of protein aqueous properties (e.g., conformation and aggregation). Different techniques suitable for HTF analysis are discussed and some of the issues concerning implementation are presented with reference to the use of microplates.</description><subject>Aggregation</subject><subject>Biological and medical sciences</subject><subject>Calorimetry</subject><subject>Chemistry, Pharmaceutical</subject><subject>Chromatography, Liquid</subject><subject>Circular Dichroism</subject><subject>Drug Evaluation, Preclinical - methods</subject><subject>Drug Stability</subject><subject>Electrophoresis</subject><subject>Fluorescence</subject><subject>Fluorescence Polarization</subject><subject>Fluorescence Resonance Energy Transfer</subject><subject>General pharmacology</subject><subject>High throughput screening</subject><subject>Hydrogen-Ion Concentration</subject><subject>Light</subject><subject>Mass Spectrometry</subject><subject>Medical sciences</subject><subject>Pharmaceutical Preparations - analysis</subject><subject>Pharmaceutical Preparations - chemistry</subject><subject>Pharmaceutical technology. Pharmaceutical industry</subject><subject>Pharmacology. Drug treatments</subject><subject>Physical and chemical characterization</subject><subject>Protein formulation</subject><subject>Proteins - analysis</subject><subject>Proteins - chemistry</subject><subject>Scattering, Radiation</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Spectroscopy</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Spectrum Analysis, Raman</subject><subject>Stability</subject><issn>0939-6411</issn><issn>1873-3441</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEFv1DAQhS0EokvhD3BAucAtYRw7sY24VBVQpEpwKGfLmUx2vcrGi-0g9d_jZVfqjbnM5XtPTx9jbzk0HHj_cd_Q_jg0LUDfgGkAzDO24VqJWkjJn7MNGGHqXnJ-xV6ltAcAqTr9kl1xxUGV27CHO7_dVXkXw7rdHddcJYxEi1-2VZiqYwyZ_FJNIR7W2WUfliplN_jZ58dP1c_oMHt0c4VhSX6k-A9Jr9mLyc2J3lz-Nfv19cvD7V19_-Pb99ub-xplB7lG5RBNp4C4ISOEUaYXRuPAnVES0LQGsQUDetTKkCZoB9lx3SMKGvtOXLMP596y8_dKKduDT0jz7BYKa7K9liBAtwVszyDGkFKkyR6jP7j4aDnYk0u7tyeX9uTSgrHFZQm9u7Svw4HGp8hFXgHeXwCXioQpugV9euK07HoDULjPZ46Kiz-eok3oaUEafSTMdgz-fzv-AgdVkxE</recordid><startdate>20070201</startdate><enddate>20070201</enddate><creator>Capelle, Martinus A.H.</creator><creator>Gurny, Robert</creator><creator>Arvinte, Tudor</creator><general>Elsevier B.V</general><general>Elsevier Science</general><scope>IQODW</scope><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></search><sort><creationdate>20070201</creationdate><title>High throughput screening of protein formulation stability: Practical considerations</title><author>Capelle, Martinus A.H. ; Gurny, Robert ; Arvinte, Tudor</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c450t-c7acc9570e19e9339796398cb1a9740c929cc20908d879e8e02b45186cc3ed653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Aggregation</topic><topic>Biological and medical sciences</topic><topic>Calorimetry</topic><topic>Chemistry, Pharmaceutical</topic><topic>Chromatography, Liquid</topic><topic>Circular Dichroism</topic><topic>Drug Evaluation, Preclinical - methods</topic><topic>Drug Stability</topic><topic>Electrophoresis</topic><topic>Fluorescence</topic><topic>Fluorescence Polarization</topic><topic>Fluorescence Resonance Energy Transfer</topic><topic>General pharmacology</topic><topic>High throughput screening</topic><topic>Hydrogen-Ion Concentration</topic><topic>Light</topic><topic>Mass Spectrometry</topic><topic>Medical sciences</topic><topic>Pharmaceutical Preparations - analysis</topic><topic>Pharmaceutical Preparations - chemistry</topic><topic>Pharmaceutical technology. Pharmaceutical industry</topic><topic>Pharmacology. Drug treatments</topic><topic>Physical and chemical characterization</topic><topic>Protein formulation</topic><topic>Proteins - analysis</topic><topic>Proteins - chemistry</topic><topic>Scattering, Radiation</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Spectroscopy</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><topic>Spectrum Analysis, Raman</topic><topic>Stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Capelle, Martinus A.H.</creatorcontrib><creatorcontrib>Gurny, Robert</creatorcontrib><creatorcontrib>Arvinte, Tudor</creatorcontrib><collection>Pascal-Francis</collection><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><jtitle>European journal of pharmaceutics and biopharmaceutics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Capelle, Martinus A.H.</au><au>Gurny, Robert</au><au>Arvinte, Tudor</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High throughput screening of protein formulation stability: Practical considerations</atitle><jtitle>European journal of pharmaceutics and biopharmaceutics</jtitle><addtitle>Eur J Pharm Biopharm</addtitle><date>2007-02-01</date><risdate>2007</risdate><volume>65</volume><issue>2</issue><spage>131</spage><epage>148</epage><pages>131-148</pages><issn>0939-6411</issn><eissn>1873-3441</eissn><abstract>The formulation of protein drugs is a difficult and time-consuming process, mainly due to the complexity of protein structure and the very specific physical and chemical properties involved. Understanding protein degradation pathways is essential for the success of a biopharmaceutical drug. The present review concerns the application of high throughput screening techniques in protein formulation development. A protein high throughput formulation (HTF) platform is based on the use of microplates. Basically, the HTF platform consists of two parts: (i) sample preparation and (ii) sample analysis. Sample preparation involves automated systems for dispensing the drug and the formulation ingredients in both liquid and powder form. The sample analysis involves specific methods developed for each protein to investigate physical and chemical properties of the formulations in microplates. Examples are presented of the use of protein intrinsic fluorescence for the analysis of protein aqueous properties (e.g., conformation and aggregation). 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| subjects | Aggregation Biological and medical sciences Calorimetry Chemistry, Pharmaceutical Chromatography, Liquid Circular Dichroism Drug Evaluation, Preclinical - methods Drug Stability Electrophoresis Fluorescence Fluorescence Polarization Fluorescence Resonance Energy Transfer General pharmacology High throughput screening Hydrogen-Ion Concentration Light Mass Spectrometry Medical sciences Pharmaceutical Preparations - analysis Pharmaceutical Preparations - chemistry Pharmaceutical technology. Pharmaceutical industry Pharmacology. Drug treatments Physical and chemical characterization Protein formulation Proteins - analysis Proteins - chemistry Scattering, Radiation Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Spectroscopy Spectroscopy, Fourier Transform Infrared Spectrum Analysis, Raman Stability |
| title | High throughput screening of protein formulation stability: Practical considerations |
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