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- W2013924294 abstract "Glycine is extensively used as an excipient in protein formulations. However, it absorbs significant infrared (IR) radiation in the conformationally sensitive amide I region (1700–1600 cm−1) of proteins. Furthermore, glycine can form a number of polymorphs, as well as an amorphous phase. Each of these forms possibly exhibits a different IR absorption spectrum. Accurate subtraction of glycine signals, in order to obtain reliable amide I spectra, was found to be possible only if the protein-to-glycine ratio was ≥1:1. In those cases, the solid-state conformation of the protein could be determined. In addition, a new method for estimating the degree of crystallinity of freeze-dried glycine is described, using IR bands in the 1350–1300 cm−1 region. © 2004 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 93:1359–1366, 2004" @default.
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- W2013924294 date "2004-05-01" @default.
- W2013924294 modified "2023-10-14" @default.
- W2013924294 title "Infrared spectroscopic studies of protein formulations containing glycine" @default.
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- W2013924294 doi "https://doi.org/10.1002/jps.20019" @default.
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