Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation.
Recent studies have clearly demonstrated that Fourier transform IR spectroscopy can be a powerful tool for the study of protein stabilization during freeze-drying and for optimizing approaches to prevent lyophilization-induced protein aggregation. The purpose of the current review is to provide an overview of these topics, as well as an introduction to the study of protein secondary structure with IR spectroscopy. We will start with a general summary of the theories and practices for processing and interpreting protein IR spectra. We will then review the current literature on the use of IR spectroscopy to study protein structure and the effects of stabilizers during lyophilization. Next we will concentrate specifically on protein aggregation. The bulk of the research and the key assignments of spectral features in protein aggregates come from studies of the effects of high and low temperature on proteins. Therefore, we will first consider this topic. Finally, we will summarize the recent theoretical and applied work on lyophilization-induced aggregation.
Dong
A
A
Department of Pharmaceutical Sciences, School of Pharmacy, University of Colorado Health Sciences Center, Denver 80262, USA.
Prestrelski
S J
SJ
Allison
S D
SD
Carpenter
J F
JF
D002918:Chymotrypsin / Q000737:chemistry; D005612:Freeze Drying; D007770:L-Lactate Dehydrogenase / Q000737:chemistry; D010732:Phosphofructokinase-1 / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D013055:Spectrophotometry, Infrared; D013696:Temperature; D013861:Thiocyanates / Q000737:chemistry
D011506:Proteins; D013861:Thiocyanates; D007770:L-Lactate Dehydrogenase; D010732:Phosphofructokinase-1; D002918:Chymotrypsin