| Autor: |
Meyer, Jeffrey D., Jun Bai, Shu, Rani, Meena, Suryanarayanan, Raj, Nayar, Rajiv, Carpenter, John F., Manning, Mark C. |
| Zdroj: |
Journal of Pharmaceutical Sciences; May 2004, Vol. 93 Issue: 5 p1359-1366, 8p |
| Abstrakt: |
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−1region. © 2004 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 93:1359–1366, 2004 |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
Plný text