Electrospray–differential mobility analysis as an orthogonal tool to size‐exclusion chromatography for characterization of protein aggregates
Identifieur interne : 002381 ( Main/Exploration ); précédent : 002380; suivant : 002382Electrospray–differential mobility analysis as an orthogonal tool to size‐exclusion chromatography for characterization of protein aggregates
Auteurs : Suvajyoti Guha [États-Unis] ; Joshua R. Wayment [États-Unis] ; Michael J. Tarlov [États-Unis] ; Michael R. Zachariah [États-Unis]Source :
- Journal of Pharmaceutical Sciences [ 0022-3549 ] ; 2012-06.
English descriptors
- Teeft :
- Adsorption, Aggregate, Aggregate formation, Aggregation, American pharmacists association, Ammonium, Ammonium acetate buffer, Anal chem, Analytical ultracentrifugation, Apparent rate, Background noise, Biopharmaceutical industry, Biotechnol bioeng, Bovine immunoglobulins, Condensation particle counter, Correction dimer, Detection limit, Different incubation times, Differential mobility analysis, Differential mobility analyzer, Dimer, Dimer peaks, Droplet, Droplet size, Droplet sizes, Droplet volume, Electrical mobility, Electrophoretic mobility, Electrospray, Error bars, General rate equation, Globular proteins, Good agreement, Guha, Higg, High salt concentrations, Higher fraction, Immunoglobulin, Incubation, Incubation time, Incubation times, June, Large aggregates, Larger aggregates, Larger oligomers, Lower limit, Mass spectrometry, Mobility analysis, Mobility diameter, Monoclonal antibody, Monomer, Monomer counts, Monomer decay, Monomer peak, Monomer peaks, Monomer proportion, Monomer proportions, Monomer ratio, National institute, Oligomers, Orthogonal, Orthogonal tool, Other peaks, Pentamer peaks, Pharm, Pharmaceutical, Pharmaceutical sciences, Potassium phosphate, Protein adsorption, Protein aggregates, Protein aggregation, Protein particles, Protein samples, Protein therapeutics, Rate constants, Reaction order, Residue size, Rmab, Size distribution, Size distributions, Size exclusion chromatography, Sodium chloride, Subvisible particles, Such cases, Tarlov, Tetramers, Therapeutic protein products, Thermal denaturation, Trimer, Wide range, Wiley periodicals, Zachariah.
Abstract
The biopharmaceutical industry characterizes and quantifies aggregation of protein therapeutics using multiple analytical techniques to cross‐validate results. Here, we demonstrate the use of electrospray–differential mobility analysis (ES–DMA), a gas‐phase and atmospheric pressure ion‐mobility method for characterizing protein aggregates. Two immunoglobulin Gs are systematically heat treated to induce aggregation and characterized using size‐exclusion chromatography (SEC) and ES–DMA. Although ES–DMA is a gas‐phase characterization method, we find that aggregation kinetic rate constants determined by ES–DMA is in good agreement with those determined by SEC. ES–DMA appears to have a higher resolution and lower limit of detection as compared with SEC. Thus, ES–DMA can potentially become an important orthogonal tool for characterization of nascent protein aggregates in the biopharmaceutical industry. © 2012 Wiley Periodicals, Inc. and the American Pharmacists Association J Pharm Sci 101:1985–1994, 2012
Url:
DOI: 10.1002/jps.23097
Affiliations:
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Here, we demonstrate the use of electrospray–differential mobility analysis (ES–DMA), a gas‐phase and atmospheric pressure ion‐mobility method for characterizing protein aggregates. Two immunoglobulin Gs are systematically heat treated to induce aggregation and characterized using size‐exclusion chromatography (SEC) and ES–DMA. Although ES–DMA is a gas‐phase characterization method, we find that aggregation kinetic rate constants determined by ES–DMA is in good agreement with those determined by SEC. ES–DMA appears to have a higher resolution and lower limit of detection as compared with SEC. Thus, ES–DMA can potentially become an important orthogonal tool for characterization of nascent protein aggregates in the biopharmaceutical industry. © 2012 Wiley Periodicals, Inc. and the American Pharmacists Association J Pharm Sci 101:1985–1994, 2012</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><country name="États-Unis"><region name="Maryland"><name sortKey="Guha, Suvajyoti" sort="Guha, Suvajyoti" uniqKey="Guha S" first="Suvajyoti" last="Guha">Suvajyoti Guha</name></region><name sortKey="Guha, Suvajyoti" sort="Guha, Suvajyoti" uniqKey="Guha S" first="Suvajyoti" last="Guha">Suvajyoti Guha</name><name sortKey="Tarlov, Michael J" sort="Tarlov, Michael J" uniqKey="Tarlov M" first="Michael J." last="Tarlov">Michael J. Tarlov</name><name sortKey="Wayment, Joshua R" sort="Wayment, Joshua R" uniqKey="Wayment J" first="Joshua R." last="Wayment">Joshua R. Wayment</name><name sortKey="Zachariah, Michael R" sort="Zachariah, Michael R" uniqKey="Zachariah M" first="Michael R." last="Zachariah">Michael R. Zachariah</name><name sortKey="Zachariah, Michael R" sort="Zachariah, Michael R" uniqKey="Zachariah M" first="Michael R." last="Zachariah">Michael R. Zachariah</name><name sortKey="Zachariah, Michael R" sort="Zachariah, Michael R" uniqKey="Zachariah M" first="Michael R." last="Zachariah">Michael R. Zachariah</name><name sortKey="Zachariah, Michael R" sort="Zachariah, Michael R" uniqKey="Zachariah M" first="Michael R." last="Zachariah">Michael R. Zachariah</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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