메뉴 건너뛰기




Volumn 51, Issue 1, 2010, Pages 39-45

Implementation of an FTIR calibration curve for fast and objective determination of changes in protein secondary structure during formulation development

Author keywords

Calibration curve; Circular dichroism; FTIR; Multivariate data analysis; Protein formulation; Secondary structure

Indexed keywords

GLUCAGON; HUMAN SERUM ALBUMIN;

EID: 70349314315     PISSN: 07317085     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jpba.2009.07.031     Document Type: Article
Times cited : (59)

References (34)
  • 1
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int. J. Pharm. 185 (1999) 129-188
    • (1999) Int. J. Pharm. , vol.185 , pp. 129-188
    • Wang, W.1
  • 2
    • 0034255393 scopus 로고    scopus 로고
    • Lyophilization and development of solid protein pharmaceuticals
    • Wang W. Lyophilization and development of solid protein pharmaceuticals. Int. J. Pharm. 203 (2000) 1-60
    • (2000) Int. J. Pharm. , vol.203 , pp. 1-60
    • Wang, W.1
  • 3
    • 0028337475 scopus 로고
    • Application of accelerated testing to shelf-life prediction of commercial protein preparations
    • Yoshioka S., and Aso Y. Application of accelerated testing to shelf-life prediction of commercial protein preparations. J. Pharm. Sci. 83 (1994) 454-456
    • (1994) J. Pharm. Sci. , vol.83 , pp. 454-456
    • Yoshioka, S.1    Aso, Y.2
  • 4
    • 0031734413 scopus 로고    scopus 로고
    • Effect of excipients on the stability and structure of lyophilized recombinant human growth hormone
    • Costantino H.R., and Carrasquillo K.G. Effect of excipients on the stability and structure of lyophilized recombinant human growth hormone. J. Pharm. Sci. 87 (1998) 1412-1420
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1412-1420
    • Costantino, H.R.1    Carrasquillo, K.G.2
  • 5
    • 0032078387 scopus 로고    scopus 로고
    • Application of infrared spectroscopy to development of stable lyophilized protein formulations
    • Carpenter J.F., and Prestrelski S.J. Application of infrared spectroscopy to development of stable lyophilized protein formulations. Eur. J. Pharm. Biopharm. 45 (1998) 231-238
    • (1998) Eur. J. Pharm. Biopharm. , vol.45 , pp. 231-238
    • Carpenter, J.F.1    Prestrelski, S.J.2
  • 6
    • 70349339414 scopus 로고    scopus 로고
    • Impact of sucrose level on storage stability of proteins in freeze-dried solids: I. Correlation of protein-sugar interaction with native structure preservation
    • published online
    • Wang B.S., and Tchessalov S. Impact of sucrose level on storage stability of proteins in freeze-dried solids: I. Correlation of protein-sugar interaction with native structure preservation. J. Pharm. Sci. (2008) published online
    • (2008) J. Pharm. Sci.
    • Wang, B.S.1    Tchessalov, S.2
  • 7
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • Arrondo J.L., and Muga A. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog. Biophys. Mol. Biol. 59 (1993) 23-56
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.1    Muga, A.2
  • 8
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth A., and Zscherp C. What vibrations tell us about proteins. Q. Rev. Biophys. 35 (2002) 369-430
    • (2002) Q. Rev. Biophys. , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 9
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler D.M., and Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25 (1986) 469-487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 10
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation
    • Dong A., and Prestrelski S.J. Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J. Pharm. Sci. 84 (1995) 415-424
    • (1995) J. Pharm. Sci. , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2
  • 11
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson M., and Mantsch H.H. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30 (1995) 95-120
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 12
    • 0030059491 scopus 로고    scopus 로고
    • Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states
    • Kendrick B.S., and Dong A. Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states. J. Pharm. Sci. 85 (1996) 155-158
    • (1996) J. Pharm. Sci. , vol.85 , pp. 155-158
    • Kendrick, B.S.1    Dong, A.2
  • 13
    • 0030271385 scopus 로고    scopus 로고
    • Secondary structure determination of proteins in aqueous solution by infrared spectroscopy: a comparison of multivariate data analysis methods
    • Rahmelow K., and Hubner W. Secondary structure determination of proteins in aqueous solution by infrared spectroscopy: a comparison of multivariate data analysis methods. Anal. Biochem. 241 (1996) 5-13
    • (1996) Anal. Biochem. , vol.241 , pp. 5-13
    • Rahmelow, K.1    Hubner, W.2
  • 14
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases
    • Whitmore L. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89 (2008) 392-400
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1
  • 15
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of helical and strand segments in proteins using CD spectroscopy
    • Sreerema N. Estimation of the number of helical and strand segments in proteins using CD spectroscopy. Protein Sci. 8 (1999) 370-380
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerema, N.1
  • 16
    • 33747855587 scopus 로고    scopus 로고
    • A reference database for circular dichroism spectroscopy covering fold and secondary structure space
    • Lees J.G. A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22 (2006) 1955-1962
    • (2006) Bioinformatics , vol.22 , pp. 1955-1962
    • Lees, J.G.1
  • 17
    • 0032029417 scopus 로고    scopus 로고
    • FTIR/ATR for protein adsorption to biomaterial surfaces
    • Chittur K.K. FTIR/ATR for protein adsorption to biomaterial surfaces. Biomaterials 19 (1998) 357-369
    • (1998) Biomaterials , vol.19 , pp. 357-369
    • Chittur, K.K.1
  • 18
    • 0024999461 scopus 로고
    • Determination of protein secondary structure using factor analysis of infrared spectra
    • Lee D.C., and Haris P.I. Determination of protein secondary structure using factor analysis of infrared spectra. Biochemistry 29 (1990) 9185-9193
    • (1990) Biochemistry , vol.29 , pp. 9185-9193
    • Lee, D.C.1    Haris, P.I.2
  • 19
    • 0024997389 scopus 로고
    • 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
    • Dousseau F., and Pezolet M. 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. Biochemistry 29 (1990) 8771-8779
    • (1990) Biochemistry , vol.29 , pp. 8771-8779
    • Dousseau, F.1    Pezolet, M.2
  • 20
    • 0025693227 scopus 로고
    • 2O) solutions. III. Estimation of the protein secondary structure
    • 2O) solutions. III. Estimation of the protein secondary structure. Biopolymers 30 (1990) 1273-1280
    • (1990) Biopolymers , vol.30 , pp. 1273-1280
    • Kalnin, N.N.1    Baikalov, I.A.2
  • 21
    • 0025906210 scopus 로고
    • Protein secondary structure from Fourier transform infrared spectroscopy: a data base analysis
    • Sarver Jr. R.W., and Krueger W.C. Protein secondary structure from Fourier transform infrared spectroscopy: a data base analysis. Anal. Biochem. 194 (1991) 89-100
    • (1991) Anal. Biochem. , vol.194 , pp. 89-100
    • Sarver Jr., R.W.1    Krueger, W.C.2
  • 22
    • 0032524420 scopus 로고    scopus 로고
    • Protein structure in KBr pellets by infrared spectroscopy
    • Forato L.A., and Bernardes-Filho R. Protein structure in KBr pellets by infrared spectroscopy. Anal. Biochem. 259 (1998) 136-141
    • (1998) Anal. Biochem. , vol.259 , pp. 136-141
    • Forato, L.A.1    Bernardes-Filho, R.2
  • 23
    • 54949141071 scopus 로고    scopus 로고
    • Determination of the secondary structure of proteins in different environments by FTIR-ATR spectroscopy and PLS regression
    • Wang Y., and Boysen R.I. Determination of the secondary structure of proteins in different environments by FTIR-ATR spectroscopy and PLS regression. Biopolymers 89 (2008) 895-905
    • (2008) Biopolymers , vol.89 , pp. 895-905
    • Wang, Y.1    Boysen, R.I.2
  • 24
    • 85151711359 scopus 로고
    • A theoretical foundation for the PLS algorithm
    • Lorber A. A theoretical foundation for the PLS algorithm. J. Chemometr. 1 (1987) 19-31
    • (1987) J. Chemometr. , vol.1 , pp. 19-31
    • Lorber, A.1
  • 25
    • 0024826939 scopus 로고
    • Underlying assumptions in the estimation of secondary structure content in proteins by circular dichroism spectroscopy-a critical review
    • Manning M.C. Underlying assumptions in the estimation of secondary structure content in proteins by circular dichroism spectroscopy-a critical review. J. Pharm. Biomed. Anal. 7 (1989) 1103-1119
    • (1989) J. Pharm. Biomed. Anal. , vol.7 , pp. 1103-1119
    • Manning, M.C.1
  • 26
    • 0017701604 scopus 로고
    • Automatic identification of secondary structure in globular proteins
    • Levitt M., and Greer J. Automatic identification of secondary structure in globular proteins. J. Mol. Biol. 114 (1977) 181-239
    • (1977) J. Mol. Biol. , vol.114 , pp. 181-239
    • Levitt, M.1    Greer, J.2
  • 27
    • 11144304496 scopus 로고    scopus 로고
    • Application of the local regression method interval partial least-squares to the elucidation of protein secondary structure
    • Navea S., and Tauler R. Application of the local regression method interval partial least-squares to the elucidation of protein secondary structure. Anal. Biochem. 336 (2005) 231-242
    • (2005) Anal. Biochem. , vol.336 , pp. 231-242
    • Navea, S.1    Tauler, R.2
  • 28
    • 0023377695 scopus 로고
    • Thermal denaturation of globular proteins. Fourier transform-infrared studies of the amide III spectral region
    • Anderle G., and Mendelsohn R. Thermal denaturation of globular proteins. Fourier transform-infrared studies of the amide III spectral region. Biophys. J. 52 (1987) 69-74
    • (1987) Biophys. J. , vol.52 , pp. 69-74
    • Anderle, G.1    Mendelsohn, R.2
  • 29
    • 0031626689 scopus 로고    scopus 로고
    • Predictions of protein secondary structures using factor analysis on Fourier transform infrared spectra: effect of Fourier self-deconvolution of the amide I and amide II bands
    • Wi S., and Pancoska P. Predictions of protein secondary structures using factor analysis on Fourier transform infrared spectra: effect of Fourier self-deconvolution of the amide I and amide II bands. Biospectroscopy 4 (1998) 93-106
    • (1998) Biospectroscopy , vol.4 , pp. 93-106
    • Wi, S.1    Pancoska, P.2
  • 30
    • 0000012892 scopus 로고
    • DSC studies on the denaturation and aggregation of serum albumins
    • Barone G. DSC studies on the denaturation and aggregation of serum albumins. Thermochim. Acta 199 (1992) 197-205
    • (1992) Thermochim. Acta , vol.199 , pp. 197-205
    • Barone, G.1
  • 31
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int. J. Pharm. 289 (2005) 1-30
    • (2005) Int. J. Pharm. , vol.289 , pp. 1-30
    • Wang, W.1
  • 32
    • 3242735868 scopus 로고    scopus 로고
    • Mishandling of the therapeutic peptide glucagon generates cytotoxic amyloidogenic fibrils
    • Onoue S. Mishandling of the therapeutic peptide glucagon generates cytotoxic amyloidogenic fibrils. Pharm. Res. 21 (2004) 1274-1283
    • (2004) Pharm. Res. , vol.21 , pp. 1274-1283
    • Onoue, S.1
  • 33
    • 0017700305 scopus 로고
    • Conformational transitions of glucagon in solution: the alpha to beta transition
    • Moran E.C. Conformational transitions of glucagon in solution: the alpha to beta transition. Biochem. Biophys. Res. Commun. 77 (1977) 1300-1306
    • (1977) Biochem. Biophys. Res. Commun. , vol.77 , pp. 1300-1306
    • Moran, E.C.1
  • 34
    • 33644816467 scopus 로고    scopus 로고
    • Structural transition of glucagon in the concentrated solution observed by electrophoretic and spectroscopic techniques
    • Onoue S. Structural transition of glucagon in the concentrated solution observed by electrophoretic and spectroscopic techniques. J. Chromatogr. A 1109 (2006) 167-173
    • (2006) J. Chromatogr. A , vol.1109 , pp. 167-173
    • Onoue, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.