메뉴 건너뛰기




Volumn 330, Issue 1-2, 2007, Pages 89-98

Characterisation and physical stability of PEGylated glucagon

Author keywords

Fibrillation; Freeze drying; Glucagon; PEGylation; Physical stability; Secondary structure

Indexed keywords

GLUCAGON; LYSINE; MACROGOL DERIVATIVE; THIOFLAVINE;

EID: 33846186433     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2006.09.002     Document Type: Article
Times cited : (38)

References (46)
  • 1
    • 0032211606 scopus 로고    scopus 로고
    • Polyethylene glycol-conjugated pharmaceutical proteins
    • Bailon P., and Berthold W. Polyethylene glycol-conjugated pharmaceutical proteins. Pharm. Sci. Technol. Today 1 (1998) 352-356
    • (1998) Pharm. Sci. Technol. Today , vol.1 , pp. 352-356
    • Bailon, P.1    Berthold, W.2
  • 2
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth A., and Zscherp C. What vibrations tell us about proteins. Quart. Rev. Biophys. 35 (2002) 369-430
    • (2002) Quart. Rev. Biophys. , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 3
    • 0014599351 scopus 로고
    • Formation and structure of gels and fibrils from glucagon
    • Beaven G.H., Gratzer W.B., and Davies H.G. Formation and structure of gels and fibrils from glucagon. Eur. J. Biochem. 11 (1969) 37-42
    • (1969) Eur. J. Biochem. , vol.11 , pp. 37-42
    • Beaven, G.H.1    Gratzer, W.B.2    Davies, H.G.3
  • 4
    • 0036155132 scopus 로고    scopus 로고
    • Pegnology: a review of PEGylated systems
    • Bhadra D., Bhadra S., Jain P., and Jain N.K. Pegnology: a review of PEGylated systems. Pharmazie 57 (2002) 5-29
    • (2002) Pharmazie , vol.57 , pp. 5-29
    • Bhadra, D.1    Bhadra, S.2    Jain, P.3    Jain, N.K.4
  • 5
    • 33846202411 scopus 로고
    • The conformation of glucagon
    • Lefébvre P.J. (Ed), Springer-Verlag, Germany
    • Blundell T.L. The conformation of glucagon. In: Lefébvre P.J. (Ed). Glucagon vol. 1 (1983), Springer-Verlag, Germany 37-56
    • (1983) Glucagon , vol.1 , pp. 37-56
    • Blundell, T.L.1
  • 6
    • 0016687342 scopus 로고
    • The conformation of glucagon: predictions and consequences
    • Chou P.Y., and Fasman G.D. The conformation of glucagon: predictions and consequences. Biochemistry 14 (1975) 2536-2541
    • (1975) Biochemistry , vol.14 , pp. 2536-2541
    • Chou, P.Y.1    Fasman, G.D.2
  • 8
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong A., Huang P., and Caughey W.S. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29 (1990) 3303-3308
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 9
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: a formulation challenge
    • Frokjaer S., and Otzen D.E. Protein drug stability: a formulation challenge. Nat. Rev. Drug Discov. 4 (2005) 298-306
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 10
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • Glasoe P.K., and Long F.A. Use of glass electrodes to measure acidities in deuterium oxide. J. Phys. Chem. 64 (1960) 188-189
    • (1960) J. Phys. Chem. , vol.64 , pp. 188-189
    • Glasoe, P.K.1    Long, F.A.2
  • 11
    • 0014691347 scopus 로고
    • Relation between conformation and association state. A study of the association equilibrium of glucagon
    • Gratzer W.B., and Beaven G.H. Relation between conformation and association state. A study of the association equilibrium of glucagon. J. Biol. Chem. 244 (1969) 6675-6679
    • (1969) J. Biol. Chem. , vol.244 , pp. 6675-6679
    • Gratzer, W.B.1    Beaven, G.H.2
  • 14
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • Haris P.I., and Chapman D. The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers 37 (1995) 251-263
    • (1995) Biopolymers , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 15
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper J.D., and Lansbury Jr. P.T. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66 (1997) 385-407
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 16
    • 0037362655 scopus 로고    scopus 로고
    • Effect of PEGylation on pharmaceuticals
    • Harris J.M., and Chess R.B. Effect of PEGylation on pharmaceuticals. Nat. Rev. Drug Discov. 2 (2003) 214-221
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 17
    • 0033230235 scopus 로고    scopus 로고
    • Investigations into the thermodynamics of polypeptide interaction with non-polar ligands
    • Hearn M.T., and Zhao G. Investigations into the thermodynamics of polypeptide interaction with non-polar ligands. Anal. Chem. 71 (1999) 4874-4885
    • (1999) Anal. Chem. , vol.71 , pp. 4874-4885
    • Hearn, M.T.1    Zhao, G.2
  • 18
    • 0037124501 scopus 로고    scopus 로고
    • Effects of PEG conjugation on insulin properties
    • Hinds K.D., and Kim S.W. Effects of PEG conjugation on insulin properties. Adv. Drug Deliv. Rev. 54 (2002) 505-530
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 505-530
    • Hinds, K.D.1    Kim, S.W.2
  • 19
    • 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
  • 20
    • 0034947503 scopus 로고    scopus 로고
    • Mass spectrometry for protein and peptide characterisation
    • Johnsson A.P. Mass spectrometry for protein and peptide characterisation. Cell. Mol. Life Sci. 58 (2001) 868-884
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 868-884
    • Johnsson, A.P.1
  • 21
    • 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., Dong A., Allison S.D., Manning M.C., and Carpenter J.F. 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    Allison, S.D.3    Manning, M.C.4    Carpenter, J.F.5
  • 22
    • 0025880710 scopus 로고
    • Studies of peptides forming 3(10)- and alpha-helices and beta-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy
    • Kennedy D.F., Crisma M., Toniolo C., and Chapman D. Studies of peptides forming 3(10)- and alpha-helices and beta-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy. Biochemistry 30 (1991) 6541-6548
    • (1991) Biochemistry , vol.30 , pp. 6541-6548
    • Kennedy, D.F.1    Crisma, M.2    Toniolo, C.3    Chapman, D.4
  • 23
    • 0036128917 scopus 로고    scopus 로고
    • PEGylated recombinant human epidermal growth factor (rhEGF) for sustained release from biodegradable PLGA microspheres
    • Kim T.H., Lee H., and Park T.G. PEGylated recombinant human epidermal growth factor (rhEGF) for sustained release from biodegradable PLGA microspheres. Biomaterials 23 (2002) 2311-2317
    • (2002) Biomaterials , vol.23 , pp. 2311-2317
    • Kim, T.H.1    Lee, H.2    Park, T.G.3
  • 25
    • 0036288833 scopus 로고    scopus 로고
    • Preparation and characterization of mono-PEGylated epidermal growth factor: evaluation of in vitro biologic activity
    • Lee H., and Park T.G. Preparation and characterization of mono-PEGylated epidermal growth factor: evaluation of in vitro biologic activity. Pharm. Res. 19 (2002) 845-851
    • (2002) Pharm. Res. , vol.19 , pp. 845-851
    • Lee, H.1    Park, T.G.2
  • 26
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution
    • LeVine H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2 (1993) 404-410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine, H.1
  • 27
    • 4644301510 scopus 로고    scopus 로고
    • Conjugates of peptides and proteins to polyethylene glycol
    • Morpurgo M., and Veronese F.M. Conjugates of peptides and proteins to polyethylene glycol. Methods Mol. Biol. 283 (2004) 45-70
    • (2004) Methods Mol. Biol. , vol.283 , pp. 45-70
    • Morpurgo, M.1    Veronese, F.M.2
  • 28
    • 0035871896 scopus 로고    scopus 로고
    • Identification of the modifying sites of mono-PEGylated salmon calcitonins by capillary electrophoresis and MALDI-TOF mass spectrometry
    • Na D.H., Park M.O., Choi S.Y., Kim Y.S., Lee S.S., Yoo S.D., Lee H.S., and Lee K.C. Identification of the modifying sites of mono-PEGylated salmon calcitonins by capillary electrophoresis and MALDI-TOF mass spectrometry. J. Chromatogr. B 754 (2001) 259-263
    • (2001) J. Chromatogr. B , vol.754 , pp. 259-263
    • Na, D.H.1    Park, M.O.2    Choi, S.Y.3    Kim, Y.S.4    Lee, S.S.5    Yoo, S.D.6    Lee, H.S.7    Lee, K.C.8
  • 29
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
    • Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., Vyas S., Uversky V.N., and Fink A.L. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40 (2001) 6036-6046
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 30
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson M.R. Techniques to study amyloid fibril formation in vitro. Methods 34 (2004) 151-160
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 31
    • 0033579545 scopus 로고    scopus 로고
    • Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin
    • Nilsson M.R., and Raleigh D.P. Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin. J. Mol. Biol. 294 (1999) 1375-1385
    • (1999) J. Mol. Biol. , vol.294 , pp. 1375-1385
    • Nilsson, M.R.1    Raleigh, D.P.2
  • 32
    • 0026124772 scopus 로고
    • The therapeutic value of poly(ethylene glycol)-modified proteins
    • Nucci M.L., Shorr R., and Abuchowski A. The therapeutic value of poly(ethylene glycol)-modified proteins. Adv. Drug Deliv. Rev. 6 (1991) 133-151
    • (1991) Adv. Drug Deliv. Rev. , vol.6 , pp. 133-151
    • Nucci, M.L.1    Shorr, R.2    Abuchowski, A.3
  • 33
    • 1642417648 scopus 로고    scopus 로고
    • Amyloid fibrils from the viewpoint of protein folding
    • Ohnishi S., and Takano K. Amyloid fibrils from the viewpoint of protein folding. Cell. Mol. Life Sci. 61 (2004) 511-524
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 511-524
    • Ohnishi, S.1    Takano, K.2
  • 35
    • 0030964876 scopus 로고    scopus 로고
    • Preparation of excipient-free recombinant human tissue-type plasminogen activator by lyophilization from ammonium bicarbonate solution: an investigation of the two-stage sublimation phenomenon
    • Overcashier D.E., Brooks D.A., Costantino H.R., and Hsu C.C. Preparation of excipient-free recombinant human tissue-type plasminogen activator by lyophilization from ammonium bicarbonate solution: an investigation of the two-stage sublimation phenomenon. J. Pharm. Sci. 86 (1997) 455-459
    • (1997) J. Pharm. Sci. , vol.86 , pp. 455-459
    • Overcashier, D.E.1    Brooks, D.A.2    Costantino, H.R.3    Hsu, C.C.4
  • 36
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 37
    • 0016146531 scopus 로고
    • Conformational nature of monomeric glucagon
    • Panijpan B., and Gratzer W.B. Conformational nature of monomeric glucagon. Eur. J. Biochem. 45 (1974) 547-553
    • (1974) Eur. J. Biochem. , vol.45 , pp. 547-553
    • Panijpan, B.1    Gratzer, W.B.2
  • 39
    • 0020413662 scopus 로고
    • Secondary structure and dynamics of glucagon in solution
    • Tran C.D., Beddard G.S., and Osborne A.D. Secondary structure and dynamics of glucagon in solution. Biochim. Biophys. Acta 709 (1982) 256-264
    • (1982) Biochim. Biophys. Acta , vol.709 , pp. 256-264
    • Tran, C.D.1    Beddard, G.S.2    Osborne, A.D.3
  • 40
    • 0035284411 scopus 로고    scopus 로고
    • Peptide and protein PEGylation: a review of problems and solutions
    • Veronese F.M. Peptide and protein PEGylation: a review of problems and solutions. Biomaterials 22 (2001) 405-417
    • (2001) Biomaterials , vol.22 , pp. 405-417
    • Veronese, F.M.1
  • 41
    • 0037124473 scopus 로고    scopus 로고
    • Introduction and overview of peptide and protein PEGylation
    • Veronese F.M., and Harris J.M. Introduction and overview of peptide and protein PEGylation. Adv. Drug Deliv. Rev. 54 (2002) 453-456
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 453-456
    • Veronese, F.M.1    Harris, J.M.2
  • 42
    • 0032870935 scopus 로고    scopus 로고
    • Bioconjugation in pharmaceutical chemistry
    • Veronese F.M., and Morpurgo M. Bioconjugation in pharmaceutical chemistry. Farmaco 54 (1999) 497-516
    • (1999) Farmaco , vol.54 , pp. 497-516
    • Veronese, F.M.1    Morpurgo, M.2
  • 44
    • 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
  • 45
    • 0020445255 scopus 로고
    • Lipid-induced ordered conformation of some peptide hormones and bioactive oligopeptides: predominance of helix over beta form
    • Wu C.S., Hachimori A., and Yang J.T. Lipid-induced ordered conformation of some peptide hormones and bioactive oligopeptides: predominance of helix over beta form. Biochemistry 21 (1982) 4556-4562
    • (1982) Biochemistry , vol.21 , pp. 4556-4562
    • Wu, C.S.1    Hachimori, A.2    Yang, J.T.3
  • 46
    • 0019310670 scopus 로고
    • Helical conformation of glucagon in surfactant solutions
    • Wu C.S., and Yang J.T. Helical conformation of glucagon in surfactant solutions. Biochemistry 19 (1980) 2117-2122
    • (1980) Biochemistry , vol.19 , pp. 2117-2122
    • Wu, C.S.1    Yang, J.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.