Thermal and FTIR investigation of freeze-dried protein-excipient mixtures
The effect of excipients on the secondary structure of lyophilized proteins was studied through second-derivative Fourier transform infrared (FTIR) spectroscopic analysis. The glass transition temperature (T g), denaturation temperature (T d) and moisture content were determined by differential scan...
Saved in:
Published in: | Journal of thermal analysis and calorimetry Vol. 89; no. 3; pp. 913 - 919 |
---|---|
Main Authors: | , , , |
Format: | Journal Article |
Language: | English |
Published: |
Dordrecht
Springer
01-09-2007
|
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | The effect of excipients on the secondary structure of lyophilized proteins was studied through second-derivative Fourier transform infrared (FTIR) spectroscopic analysis. The glass transition temperature (T g), denaturation temperature (T d) and moisture content were determined by differential scanning calorimetry (DSC) and thermogravimetry (TG). T g, T d and the preservation of protein secondary structure were found to be dependent upon the type and amount of the excipient included in the formulation. Meanwhile, the lyophilized proteins easily adsorbed amounts of moisture during storage to reduce their T gs and stability. |
---|---|
Bibliography: | SourceType-Scholarly Journals-2 ObjectType-Feature-2 ObjectType-Conference Paper-1 content type line 23 SourceType-Conference Papers & Proceedings-1 ObjectType-Article-3 |
ISSN: | 1388-6150 1588-2926 1572-8943 |
DOI: | 10.1007/s10973-006-7598-y |