Fourier-Transform Midinfrared Spectroscopy for Analysis and Screening of Liquid Protein Formulations Part 2 : Detailed Analysis and Applications

LEVEL: ADVANCED I n the first half of this two-part article (1), we introduced the physical principle behind infrared (IR) absorptions and experimental setups used for investigating protein samples. This second part concludes by focusing on the use of IR spectroscopic data in formulation stability studies and for characterizing protein secondary structures and related changes (e.g., resulting from protein–excipient interactions). We also examine IR’s use in screening protein formulations.

[1]  Joachim A Hering,et al.  Neuro‐fuzzy structural classification of proteins for improved protein secondary structure prediction , 2003, Proteomics.

[2]  B D Ratner,et al.  IR spectral changes of bovine serum albumin upon surface adsorption. , 1989, Journal of biomedical materials research.

[3]  A. Barth,et al.  What vibrations tell about proteins , 2002, Quarterly Reviews of Biophysics.

[4]  M. Pézolet,et al.  Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods. , 1990, Biochemistry.

[5]  Isao Noda,et al.  Advances in two-dimensional correlation spectroscopy , 2004 .

[6]  Erik Goormaghtigh,et al.  Rationally selected basis proteins: A new approach to selecting proteins for spectroscopic secondary structure analysis , 2003, Protein science : a publication of the Protein Society.

[7]  J. Bandekar,et al.  Amide modes and protein conformation. , 1992, Biochimica et biophysica acta.

[8]  P. Innocent,et al.  Beyond average protein secondary structure content prediction using FTIR spectroscopy , 2004, Applied bioinformatics.

[9]  Fen-Ni Fu,et al.  Secondary Structure Estimation of Proteins Using the Amide III Region of Fourier Transform Infrared Spectroscopy: Application to Analyze Calcium-Binding-Induced Structural Changes in Calsequestrin , 1994 .

[10]  W. Hübner,et al.  Secondary structure determination of proteins in aqueous solution by infrared spectroscopy: a comparison of multivariate data analysis methods. , 1996, Analytical biochemistry.

[11]  K. Griebenow,et al.  Structure Analysis of Dipeptides in Water by Exploring and Utilizing the Structural Sensitivity of Amide III by Polarized Visible Raman, FTIR−Spectroscopy and DFT Based Normal Coordinate Analysis , 2002 .

[12]  R. Jakobsen,et al.  An Algorithm for the Reproducible Spectral Subtraction of Water from the FT-IR Spectra of Proteins in Dilute Solutions and Adsorbed Monolayers , 1986 .

[13]  M. Manning,et al.  Aggregation of recombinant human interferon gamma: kinetics and structural transitions. , 1998, Journal of pharmaceutical sciences.

[14]  S. Venyaminov,et al.  Determination of Protein Secondary Structure , 1996 .

[15]  H. Susi,et al.  Examination of the secondary structure of proteins by deconvolved FTIR spectra , 1986, Biopolymers.

[16]  P. Garidel,et al.  Conformational analysis of protein secondary structure during spray-drying of antibody/mannitol formulations. , 2007, European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V.

[17]  J. Bandekar,et al.  Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. , 1986, Advances in protein chemistry.

[18]  J. Steinier,et al.  Smoothing and differentiation of data by simplified least square procedure. , 1972, Analytical chemistry.

[19]  Douglas J. Moffatt,et al.  Fourier Self-Deconvolution: A Method for Resolving Intrinsically Overlapped Bands , 1981 .

[20]  R. Mitchell,et al.  Determination of protein secondary structure using factor analysis of infrared spectra. , 1990, Biochemistry.

[21]  A. Savitzky,et al.  Smoothing and Differentiation of Data by Simplified Least Squares Procedures. , 1964 .

[22]  P. Innocent,et al.  Automatic amide I frequency selection for rapid quantification of protein secondary structure from Fourier transform infrared spectra of proteins , 2002, Proteomics.

[23]  T. Arakawa,et al.  Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. , 1993, Biophysical journal.

[24]  D. Moffatt,et al.  Deconvolution, Derivation, and Smoothing of Spectra Using Fourier Transforms , 1984 .

[25]  M. Cascio,et al.  Evaluation of methods for the prediction of membrane protein secondary structures. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[26]  S. Venyaminov,et al.  Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands , 1990, Biopolymers.

[27]  T. Shimanouchi,et al.  Normal Vibrations of N‐Methylacetamide , 1958 .

[28]  W. Hennink,et al.  Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors. , 2001, Analytical biochemistry.

[29]  P. Garidel,et al.  Fourier-Transform Midinfrared Spectroscopy for Analysis and Screening of Liquid Protein Formulations , Part 1 Understanding Infrared Spectroscopy of Proteins , 2006 .

[30]  E. Goormaghtigh,et al.  The optimization of protein secondary structure determination with infrared and circular dichroism spectra. , 2004, European journal of biochemistry.

[31]  P. Haris,et al.  Does Fourier-transform infrared spectroscopy provide useful information on protein structures? , 1992, Trends in biochemical sciences.

[32]  M. Manning,et al.  Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states. , 1996, Journal of pharmaceutical sciences.

[33]  W. J. DeGrip,et al.  Deconvolution as a tool to remove fringes from an FT-IR spectrum , 2004 .