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Volumn 94, Issue 12, 2005, Pages 2749-2763

Biophysical signatures of noncovalent aggregates formed by a glucagonlike peptide-1 analog: A prototypical example of biopharmaceutical aggregation

Author keywords

Aggregation; Circular; Dichroism; Fluorescence spectroscopy; FTIR; Light scattering; Peptides; Physical stability

Indexed keywords

ACETONITRILE; AMINO ACID; DYE; GLUCAGON LIKE PEPTIDE 1 DERIVATIVE; LY 307161; MONOMER;

EID: 33144465205     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.20420     Document Type: Article
Times cited : (11)

References (30)
  • 1
    • 0026596851 scopus 로고
    • Antidiabetogenic effect of glucagon-like peptide-1(7-36)amide in normal subjects and patients with diabetes mellitus
    • Gutniak M, Orskov C, Holst JJ, Ahren B, Efendic S. 1992. Antidiabetogenic effect of glucagon-like peptide-1(7-36)amide in normal subjects and patients with diabetes mellitus. N Engl J Med 326:1316-1322.
    • (1992) N Engl J Med , vol.326 , pp. 1316-1322
    • Gutniak, M.1    Orskov, C.2    Holst, J.J.3    Ahren, B.4    Efendic, S.5
  • 2
    • 0034857141 scopus 로고    scopus 로고
    • Development of glucagon-like peptide-1-based pharmaceuticals as therapeutic agents for the treatment of diabetes
    • Drucker DJ. 2001. Development of glucagon-like peptide-1-based pharmaceuticals as therapeutic agents for the treatment of diabetes. Curr Pharm Des 14:1399-1412.
    • (2001) Curr Pharm des , vol.14 , pp. 1399-1412
    • Drucker, D.J.1
  • 3
    • 0028074902 scopus 로고
    • FT-IR and Near-infrared FT-Raman studies of the secondary structure of insulinotropin in the solid state: α-helix to β-sheet conversion induced by phenol and/or by high shear force
    • Kim Y, Rose CA, Liu Y, Ozaki Y, Datta G, Tu AT. 1994. FT-IR and Near-infrared FT-Raman studies of the secondary structure of insulinotropin in the solid state: α-helix to β-sheet conversion induced by phenol and/or by high shear force. J Pharm Sci 83:1175-1180.
    • (1994) J Pharm Sci , vol.83 , pp. 1175-1180
    • Kim, Y.1    Rose, C.A.2    Liu, Y.3    Ozaki, Y.4    Datta, G.5    Tu, A.T.6
  • 5
    • 0035158301 scopus 로고    scopus 로고
    • Human immune response to recombinant human proteins
    • Porter S. 2001. Human immune response to recombinant human proteins. J Pharm Sci 90:1-11.
    • (2001) J Pharm Sci , vol.90 , pp. 1-11
    • Porter, S.1
  • 6
    • 3242892400 scopus 로고    scopus 로고
    • Immunogenicity of recombinant human proteins: Causes and consequences
    • Schellekens H, Casadevall N. 2004. Immunogenicity of recombinant human proteins: Causes and consequences. J Neurol 251:11/4-11/9.
    • (2004) J Neurol , vol.251
    • Schellekens, H.1    Casadevall, N.2
  • 9
    • 0029198722 scopus 로고
    • Degradative covalent reactions important to protein stability
    • Shirley BA, editor. Totowa: Humana Press Inc.
    • Volkin DB, Mach H, Middaugh CR. 1995. Degradative covalent reactions important to protein stability. In: Shirley BA, editor. Protein stability and folding. Totowa: Humana Press Inc., pp 35-63.
    • (1995) Protein Stability and Folding , pp. 35-63
    • Volkin, D.B.1    Mach, H.2    Middaugh, C.R.3
  • 10
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization and formulation of liquid protein pharmaceuticals
    • Wang W. 1999. Instability, stabilization and formulation of liquid protein pharmaceuticals. Int J Pharm 185:129-188.
    • (1999) Int J Pharm , vol.185 , pp. 129-188
    • Wang, W.1
  • 11
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions
    • Wen J, Arakawa T, Philo JS. 1996. Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal Biochem 240:155-166.
    • (1996) Anal Biochem , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 13
    • 0347477301 scopus 로고    scopus 로고
    • Micelle-associated protein in epoetin formulations: A risk factor for immunogenicity?
    • Hermeling S, Schellekens H, Crommelin DJA, Jiskroot W. 2003. Micelle-associated protein in epoetin formulations: A risk factor for immunogenicity? Pharm Res 20:1903-1907.
    • (2003) Pharm Res , vol.20 , pp. 1903-1907
    • Hermeling, S.1    Schellekens, H.2    Crommelin, D.J.A.3    Jiskroot, W.4
  • 14
    • 0842304936 scopus 로고    scopus 로고
    • Minimizing the immunogenicity of protein therapeutics
    • Chirino AJ, Ary ML, Marshall SA. 2004. Minimizing the immunogenicity of protein therapeutics. Drug Discov Today 9:82-90.
    • (2004) Drug Discov Today , vol.9 , pp. 82-90
    • Chirino, A.J.1    Ary, M.L.2    Marshall, S.A.3
  • 15
    • 0036861899 scopus 로고    scopus 로고
    • Immunogenicity of therapeutic proteins: Clinical implications and future prospects
    • Schellekens H. 2002. Immunogenicity of therapeutic proteins: Clinical implications and future prospects. Clin Ther 24:1720-1740.
    • (2002) Clin Ther , vol.24 , pp. 1720-1740
    • Schellekens, H.1
  • 16
    • 3342969278 scopus 로고    scopus 로고
    • When biotech proteins go off-patent
    • Schellekens H. 2004. When biotech proteins go off-patent. Trends in Biotechnology 22:406-410.
    • (2004) Trends in Biotechnology , vol.22 , pp. 406-410
    • Schellekens, H.1
  • 17
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • Shire SJ, Shahrokh Z, Liu J. 2004. Challenges in the development of high protein concentration formulations. J Pharm Sci 93:1390-1402.
    • (2004) J Pharm Sci , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 18
    • 8344224534 scopus 로고    scopus 로고
    • Characterizing biological products and assessing comparability following manufacturing changes
    • Chirino AJ, Mire-Sluis A. 2004. Characterizing biological products and assessing comparability following manufacturing changes. Nat Biotechnol 22:1383-1391.
    • (2004) Nat Biotechnol , vol.22 , pp. 1383-1391
    • Chirino, A.J.1    Mire-Sluis, A.2
  • 19
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding SE, Rowe AJ, Horton JC, editors. Cambridge, UK: The Royal Society of Chemistry
    • Laue TM, Shah B, Ridgeway TM, Pelletier SL. 1992. Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding SE, Rowe AJ, Horton JC, editors. Analytical ultracentrifugation in biochemistry and polymer science. Cambridge, UK: The Royal Society of Chemistry, pp 90-125.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 20
    • 0842289320 scopus 로고    scopus 로고
    • Effects of potassium bromide disk formation on the infrared spectra of dried model proteins
    • Meyer JD, Manning MC, Carpenter JF. 2004. Effects of potassium bromide disk formation on the infrared spectra of dried model proteins. J Pharm Sci 93:496-506.
    • (2004) J Pharm Sci , vol.93 , pp. 496-506
    • Meyer, J.D.1    Manning, M.C.2    Carpenter, J.F.3
  • 21
    • 0041413204 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic studies of peptides: Potentials and pitfalls
    • Singh BR, editor. Washington, DC: American Chemical Society
    • Haris PI. 2000. Fourier transform infrared spectroscopic studies of peptides: Potentials and pitfalls. In: Singh BR, editor. Infrared analysis of peptides and proteins Principles and applications. Washington, DC: American Chemical Society, 70p 54-95.
    • (2000) Infrared Analysis of Peptides and Proteins Principles and Applications , pp. 54-95
    • Haris, P.I.1
  • 22
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation
    • Dong A, Prestrelski SJ, Allison SD, Carpenter JF. 1995. Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J Pharm Sci 84:415-424.
    • (1995) J Pharm Sci , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 23
    • 0035158241 scopus 로고    scopus 로고
    • Studies of the structure of insulin fibrils by Fourier Transform Infrared (FTIR) Spectroscopy and Electron Microscopy
    • Nielsen L, Frokjaer S, Carpenter JF, Brange J. 2001. Studies of the structure of insulin fibrils by Fourier Transform Infrared (FTIR) Spectroscopy and Electron Microscopy. J Pharm Sci 90:29-37.
    • (2001) J Pharm Sci , vol.90 , pp. 29-37
    • Nielsen, L.1    Frokjaer, S.2    Carpenter, J.F.3    Brange, J.4
  • 24
    • 0001943903 scopus 로고    scopus 로고
    • Fluorescence spectroscopy in peptide and protein analysis
    • Meyers RA, editor. Chichester: John Wiley and Sons Ltd.
    • Ladokhin AS. 2000. Fluorescence spectroscopy in peptide and protein analysis. In: Meyers RA, editor. Encyclopedia of Analytical Chemistry. Chichester: John Wiley and Sons Ltd., pp 5762-5779.
    • (2000) Encyclopedia of Analytical Chemistry , pp. 5762-5779
    • Ladokhin, A.S.1
  • 25
    • 0027502784 scopus 로고
    • Thioflavin T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine HD. 1993. Thioflavin T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution. Protein Science 2:404-410.
    • (1993) Protein Science , vol.2 , pp. 404-410
    • Levine, H.D.1
  • 26
    • 0032899322 scopus 로고    scopus 로고
    • Quantifying amyloid β-peptide (Aβ) aggregation using the congo red-Aβ (CR-Aβ) spectrophotometric assay
    • Klunk WE, Jacob RF, Mason RP. 1999. Quantifying amyloid β-peptide (Aβ) aggregation using the congo red-Aβ (CR-Aβ) spectrophotometric assay. Anal Biochem 266:66-76.
    • (1999) Anal Biochem , vol.266 , pp. 66-76
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 27
    • 0027218994 scopus 로고
    • The application of size exclusion chromatography and computer simulation to study the thermodynamic and kinetic parameters for short-lived dissociable protein aggregates
    • Patapoff TW, Mrsny RJ, Lee WA. 1993. The application of size exclusion chromatography and computer simulation to study the thermodynamic and kinetic parameters for short-lived dissociable protein aggregates. Anal Biochem 212:71-78.
    • (1993) Anal Biochem , vol.212 , pp. 71-78
    • Patapoff, T.W.1    Mrsny, R.J.2    Lee, W.A.3
  • 29
    • 0036132087 scopus 로고    scopus 로고
    • Medium-dependence of the secondary structure of Exendin-4 and glucagon-like peptide-1
    • Andersen NH, Brodsky Y, Neidigh JW, Prickett KS. 2002. Medium-dependence of the secondary structure of Exendin-4 and glucagon-like peptide-1. Bioorg Med Chem 10:79-85.
    • (2002) Bioorg Med Chem , vol.10 , pp. 79-85
    • Andersen, N.H.1    Brodsky, Y.2    Neidigh, J.W.3    Prickett, K.S.4
  • 30
    • 0028207562 scopus 로고
    • Structure of glucagon-like peptide(7-36) amide in a dodecylphosphocholine micelle as determined by 2D NMR
    • Thornton K, Gorenstein DG. 1994. Structure of glucagon-like peptide(7-36) amide in a dodecylphosphocholine micelle as determined by 2D NMR. Biochemistry 33:3532-3539.
    • (1994) Biochemistry , vol.33 , pp. 3532-3539
    • Thornton, K.1    Gorenstein, D.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.