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• W2072065650 abstract "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 shown to be critical in optimizing protein stability during storage. In this study, an IgG1 was lyophilized with varying amounts of sucrose. In some formulations, a small amount of sorbitol was added as a plasticizer. The structure of the protein in dried state was monitored using infrared (IR) spectroscopy. The IR spectra indicated increasing retention of the native structure, which correlated with stability as indicated by size-exclusion chromatography as well as micro-flow imaging. Maximal stability was achieved with a 2:1 mass ratio of sucrose to protein, which is more than that would be expected based on earlier studies. Analysis of both high and low frequency bands associated with intramolecular β-sheet structure provides additional information on the structure of antibodies in the solid state. Finally, there is a correlation between the bandwidth of the β-sheet bands and the enthalpy of relaxation, suggesting that amide I bands can provide some indication of the degree of coupling to the sugar matrix, as well as structural heterogeneity of the protein. © 2011 Wiley Periodicals, Inc. and the American Pharmacists Association. 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 shown to be critical in optimizing protein stability during storage. In this study, an IgG1 was lyophilized with varying amounts of sucrose. In some formulations, a small amount of sorbitol was added as a plasticizer. The structure of the protein in dried state was monitored using infrared (IR) spectroscopy. The IR spectra indicated increasing retention of the native structure, which correlated with stability as indicated by size-exclusion chromatography as well as micro-flow imaging. Maximal stability was achieved with a 2:1 mass ratio of sucrose to protein, which is more than that would be expected based on earlier studies. Analysis of both high and low frequency bands associated with intramolecular β-sheet structure provides additional information on the structure of antibodies in the solid state. Finally, there is a correlation between the bandwidth of the β-sheet bands and the enthalpy of relaxation, suggesting that amide I bands can provide some indication of the degree of coupling to the sugar matrix, as well as structural heterogeneity of the protein. © 2011 Wiley Periodicals, Inc. and the American Pharmacists Association. Murphy B, Zhang N, Payne R, Davis J, Abdul-Fattah A, Matsuura J, Herman A, Manning M. 2012. Structure, Stability, and Mobility of a Lyophilized IgG1 Monoclonal Antibody as Determined using Second-Derivative Infrared Spectroscopy. J Pharm Sci 101:81–91.Journal of Pharmaceutical SciencesVol. 101Issue 5PreviewThe original article to which this erratum refers was published in 2012; 101:81–91. Full-Text PDF" @default.
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• W2072065650 date "2012-01-01" @default.
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• W2072065650 title "Structure, Stability, and Mobility of a Lyophilized IgG1 Monoclonal Antibody as Determined Using Second-Derivative Infrared Spectroscopy" @default.
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• W2072065650 doi "https://doi.org/10.1002/jps.22753" @default.
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