Infrared Spectroscopic Studies of Protein Formulations Containing Glycine

Jeffrey D. Meyer; Shu Jun Bai; Meena Rani; Raj Suryanarayanan; Rajiv Nayar; John F. Carpenter; Mark C. Manning

doi:10.1002/jps.20019

Infrared Spectroscopic Studies of Protein Formulations Containing Glycine

Jeffrey D. Meyer, Shu Jun Bai, Meena Rani, Raj Suryanarayanan, Rajiv Nayar, John F. Carpenter, Mark C. Manning

Pharmaceutics

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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.

Original language	English (US)
Pages (from-to)	1359-1366
Number of pages	8
Journal	Journal of Pharmaceutical Sciences
Volume	93
Issue number	5
DOIs	https://doi.org/10.1002/jps.20019
State	Published - May 2004

Keywords

Crystallinity
Glycine
Infrared spectroscopy
Lyophilization
Protein formulation
X-ray diffraction

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10.1002/jps.20019

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title = "Infrared Spectroscopic Studies of Protein Formulations Containing Glycine",

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.",

keywords = "Crystallinity, Glycine, Infrared spectroscopy, Lyophilization, Protein formulation, X-ray diffraction",

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T1 - Infrared Spectroscopic Studies of Protein Formulations Containing Glycine

AU - Meyer, Jeffrey D.

AU - Bai, Shu Jun

AU - Rani, Meena

AU - Suryanarayanan, Raj

AU - Nayar, Rajiv

AU - Carpenter, John F.

AU - Manning, Mark C.

PY - 2004/5

Y1 - 2004/5

N2 - 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.

AB - 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.

KW - Crystallinity

KW - Glycine

KW - Infrared spectroscopy

KW - Lyophilization

KW - Protein formulation

KW - X-ray diffraction

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JO - Journal of Pharmaceutical Sciences

JF - Journal of Pharmaceutical Sciences

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ER -

Infrared Spectroscopic Studies of Protein Formulations Containing Glycine

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