Infrared spectroscopic studies of protein formulations containing glycine
2004
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
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