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Volumn 101, Issue 6, 2012, Pages 2025-2033

Comparability of protein therapeutics: Quantitative comparison of second-derivative amide I infrared spectra

Author keywords

Area overlap; Biopharmaceuticals characterization; Comparability studies; FTIR; Higher order structures; Protein structure; Proteins; Secondary structure; Spectral correlation coefficient; Structure

Indexed keywords

AMIDE;

EID: 84859777985     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23133     Document Type: Article
Times cited : (25)

References (28)
  • 1
    • 0037453163 scopus 로고    scopus 로고
    • Secondary structure alterations in insulin and growth hormone oil-in-water emulsions
    • Jorgensen L, Vermehren C, Bjerragaard S, Frokjaer S. 2003. Secondary structure alterations in insulin and growth hormone oil-in-water emulsions. Int J Pharm 254:7-10.
    • (2003) Int J Pharm , vol.254 , pp. 7-10
    • Jorgensen, L.1    Vermehren, C.2    Bjerragaard, S.3    Frokjaer, S.4
  • 2
    • 34848843707 scopus 로고    scopus 로고
    • Effects of sugar additives on protein stability of recombinant human serum albumin during lyophilization and storage
    • Han Y, Jin BS, Lee SB, Sohn Y, Joung JW, Lee JH. 2007. Effects of sugar additives on protein stability of recombinant human serum albumin during lyophilization and storage. Arch Pharm Res 30:1124-1131.
    • (2007) Arch Pharm Res , vol.30 , pp. 1124-1131
    • Han, Y.1    Jin, B.S.2    Lee, S.B.3    Sohn, Y.4    Joung, J.W.5    Lee, J.H.6
  • 3
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. 2005. Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm 289:1-30.
    • (2005) Int J Pharm , vol.289 , pp. 1-30
    • Wang, W.1
  • 4
    • 0034129568 scopus 로고    scopus 로고
    • Stability of human serum albumin during bioprocessing: Denaturation and aggregation during processing of albumin paste
    • Lin JJ, Meyer JD, Carpenter JF, Manning MC. 2000. Stability of human serum albumin during bioprocessing: Denaturation and aggregation during processing of albumin paste. Pharm Res 17:391-396.
    • (2000) Pharm Res , vol.17 , pp. 391-396
    • Lin, J.J.1    Meyer, J.D.2    Carpenter, J.F.3    Manning, M.C.4
  • 5
    • 27144468628 scopus 로고    scopus 로고
    • Use of infrared spectroscopy to monitor protein structure and stability
    • Manning MC. 2005. Use of infrared spectroscopy to monitor protein structure and stability. Expert Rev Proteomics 2(5):731-743.
    • (2005) Expert Rev Proteomics , vol.2 , Issue.5 , pp. 731-743
    • Manning, M.C.1
  • 6
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • Surewicz WK, Mantsch HH. 1988. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim Biophys Acta 952:115-130.
    • (1988) Biochim Biophys Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 7
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier-transform IR spectroscopy
    • Haris PI, Chapman D. 1995. The conformational analysis of peptides using Fourier-transform IR spectroscopy. Biopolymers 37(4):251-263.
    • (1995) Biopolymers , vol.37 , Issue.4 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 8
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong A, Huang P, Caughey WS. 1990. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29(13):3303-3308.
    • (1990) Biochemistry , vol.29 , Issue.13 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 9
    • 0028865701 scopus 로고
    • Optimization of lyophilization conditions for recombinant human interleukin-2 by dried-state conformational-analysis using Fourier-transform infrared spectroscopy
    • Prestrelski SJ, Pikal KA, Arakawa T. 1995. Optimization of lyophilization conditions for recombinant human interleukin-2 by dried-state conformational-analysis using Fourier-transform infrared spectroscopy. Pharm Res 12(9):1250-1259.
    • (1995) Pharm Res , vol.12 , Issue.9 , pp. 1250-1259
    • Prestrelski, S.J.1    Pikal, K.A.2    Arakawa, T.3
  • 10
    • 70349314315 scopus 로고    scopus 로고
    • Implementation of an FTIR calibration curve for fast and objective determination of changes in protein secondary structure during formulation development
    • Vonhoff S, Condliffe J, Schiffter H. 2010. Implementation of an FTIR calibration curve for fast and objective determination of changes in protein secondary structure during formulation development. J Pharm Biomed Anal 51(1):39-45.
    • (2010) J Pharm Biomed Anal , vol.51 , Issue.1 , pp. 39-45
    • Vonhoff, S.1    Condliffe, J.2    Schiffter, H.3
  • 12
    • 0027163348 scopus 로고
    • Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers
    • Prestrelski SJ, Tedeschi N, Arakawa T, Carpenter JF. 1993. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophys J 65(2):661-671.
    • (1993) Biophys J , vol.65 , Issue.2 , pp. 661-671
    • Prestrelski, S.J.1    Tedeschi, N.2    Arakawa, T.3    Carpenter, J.F.4
  • 13
    • 0036929348 scopus 로고    scopus 로고
    • Structure of poly(ethylene glycol)-modified horseradish peroxidase in organic solvents: Infrared amide I spectral changes upon protein dehydration are largely caused by protein structural changes and not by water removal per se
    • Al-Azzam W, Pastrana EA, Ferrer Y, Huang Q, Schweitzer-Stenner R, Griebenow K. 2002. Structure of poly(ethylene glycol)-modified horseradish peroxidase in organic solvents: Infrared amide I spectral changes upon protein dehydration are largely caused by protein structural changes and not by water removal per se. Biophys J 83:3637-3651.
    • (2002) Biophys J , vol.83 , pp. 3637-3651
    • Al-Azzam, W.1    Pastrana, E.A.2    Ferrer, Y.3    Huang, Q.4    Schweitzer-Stenner, R.5    Griebenow, K.6
  • 14
    • 73649096180 scopus 로고    scopus 로고
    • Thermal stability and conformational structure of salmon calcitonin in the solid state and liquid states
    • Lee TH, Cheng WT, Lin SY. 2010. Thermal stability and conformational structure of salmon calcitonin in the solid state and liquid states. Biopolymers 93:200-207.
    • (2010) Biopolymers , vol.93 , pp. 200-207
    • Lee, T.H.1    Cheng, W.T.2    Lin, S.Y.3
  • 15
    • 0032078387 scopus 로고    scopus 로고
    • Application of infrared spectroscopy to development of stable lyophilized protein formulations
    • Carpenter JF, Prestrelski SJ, Dong AC. 1998. Application of infrared spectroscopy to development of stable lyophilized protein formulations. Eur J Pharm Biopharm 45(3):231-238.
    • (1998) Eur J Pharm Biopharm , vol.45 , Issue.3 , pp. 231-238
    • Carpenter, J.F.1    Prestrelski, S.J.2    Dong, A.C.3
  • 16
    • 0030059491 scopus 로고    scopus 로고
    • Quantitation of the area of overlap between second-derivative amide 1 infrared spectra to determine the structural similarity of a protein in different states
    • Kendrick BS, Dong AC, Allison SD, Manning MC, Carpenter JF. 1996. Quantitation of the area of overlap between second-derivative amide 1 infrared spectra to determine the structural similarity of a protein in different states. J Pharm Sci 85(2):155-158.
    • (1996) J Pharm Sci , vol.85 , Issue.2 , pp. 155-158
    • Kendrick, B.S.1    Dong, A.C.2    Allison, S.D.3    Manning, M.C.4    Carpenter, J.F.5
  • 17
    • 0029815193 scopus 로고    scopus 로고
    • Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying, and rehydration
    • Allison SD, Dong AC, Carpenter JF. 1996. Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying, and rehydration. Biophys J 71:2022-2032.
    • (1996) Biophys J , vol.71 , pp. 2022-2032
    • Allison, S.D.1    Dong, A.C.2    Carpenter, J.F.3
  • 18
    • 0032190182 scopus 로고    scopus 로고
    • Effects of drying methods and additives on structure and function of actin: Mechanisms of dehydration-induced damage and its inhibition
    • Allison SD, Randolph TW, Manning MC, Middleton K, Davis A, Carpenter JF. 1998. Effects of drying methods and additives on structure and function of actin: Mechanisms of dehydration-induced damage and its inhibition. Arch Biochem Biophys 358:171-181.
    • (1998) Arch Biochem Biophys , vol.358 , pp. 171-181
    • Allison, S.D.1    Randolph, T.W.2    Manning, M.C.3    Middleton, K.4    Davis, A.5    Carpenter, J.F.6
  • 19
    • 0030443488 scopus 로고    scopus 로고
    • Effects of phase separating systems on lyophilized hemoglobin
    • Heller MC, Carpenter JF, Randolph TW. 1996. Effects of phase separating systems on lyophilized hemoglobin. J Pharm Sci 85:1358-1362.
    • (1996) J Pharm Sci , vol.85 , pp. 1358-1362
    • Heller, M.C.1    Carpenter, J.F.2    Randolph, T.W.3
  • 20
    • 0029902287 scopus 로고    scopus 로고
    • On protein denaturation in aqueous-organic mixtures but not in pure organic solvents
    • Griebenow K, Klibanov AM. 1996. On protein denaturation in aqueous-organic mixtures but not in pure organic solvents. J Am Chem Soc 118:11695-11700.
    • (1996) J Am Chem Soc , vol.118 , pp. 11695-11700
    • Griebenow, K.1    Klibanov, A.M.2
  • 21
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson M, Mantsch HH. 1995. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit Rev Biochem Mol Biol 30(2):95-120.
    • (1995) Crit Rev Biochem Mol Biol , vol.30 , Issue.2 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 22
    • 15744400209 scopus 로고    scopus 로고
    • Probing conformational changes of proteins by quantitative second-derivative infrared spectroscopy
    • Zhang J, Yan YB. 2005. Probing conformational changes of proteins by quantitative second-derivative infrared spectroscopy. Anal Biochem 340(1):89-98.
    • (2005) Anal Biochem , vol.340 , Issue.1 , pp. 89-98
    • Zhang, J.1    Yan, Y.B.2
  • 23
    • 80053267911 scopus 로고    scopus 로고
    • Qualification of FTIR spectroscopic method for protein secondary structural analysis
    • Jiang Y, Li C, Nguyen X, Muzammil S, Towers E, Gabrielson J, Narhi L. 2011. Qualification of FTIR spectroscopic method for protein secondary structural analysis. J Pharm Sci 100(11):4631-4641.
    • (2011) J Pharm Sci , vol.100 , Issue.11 , pp. 4631-4641
    • Jiang, Y.1    Li, C.2    Nguyen, X.3    Muzammil, S.4    Towers, E.5    Gabrielson, J.6    Narhi, L.7
  • 24
    • 0035887070 scopus 로고    scopus 로고
    • Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling method and stress factors
    • van de Weert M, Haris PI, Hennink WE, Crommelin DJA. 2001. Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling method and stress factors. Anal Biochem 297(2):160-169.
    • (2001) Anal Biochem , vol.297 , Issue.2 , pp. 160-169
    • van de, W.M.1    Haris, P.I.2    Hennink, W.E.3    Crommelin, D.J.A.4
  • 25
    • 80053236482 scopus 로고    scopus 로고
    • Applications of circular dichroism (CD) for structural analysis of proteins: Qualification of near- and far-UVCD for protein higher order structural analysis
    • Li CH, Nguyen X, Nahri L, Chemmalil L, Towers E, Muzammil S, Gabrielson J, Jiang Y. 2011. Applications of circular dichroism (CD) for structural analysis of proteins: Qualification of near- and far-UVCD for protein higher order structural analysis. J Pharm Sci 100(11):4642-4654.
    • (2011) J Pharm Sci , vol.100 , Issue.11 , pp. 4642-4654
    • Li, C.H.1    Nguyen, X.2    Nahri, L.3    Chemmalil, L.4    Towers, E.5    Muzammil, S.6    Gabrielson, J.7    Jiang, Y.8
  • 26
    • 84926662675 scopus 로고
    • Nearest neighbor pattern classification
    • Cover TM, Hart PE. 1967. Nearest neighbor pattern classification. IEEE Trans Inf Theory 13(1):21-27.
    • (1967) IEEE Trans Inf Theory , vol.13 , Issue.1 , pp. 21-27
    • Cover, T.M.1    Hart, P.E.2
  • 27
    • 78650504301 scopus 로고    scopus 로고
    • Different solid sample preparation methods affecting the spectral similarity of salmon calcitonin
    • Lin SY, Lin CC, Lee TH. 2010. Different solid sample preparation methods affecting the spectral similarity of salmon calcitonin. Spectroscopy 24:511-516.
    • (2010) Spectroscopy , vol.24 , pp. 511-516
    • Lin, S.Y.1    Lin, C.C.2    Lee, T.H.3
  • 28
    • 80053236482 scopus 로고    scopus 로고
    • Applications of circular dichroism (CD) for structural analysis of proteins: Qualification of near- and far-UV CD for protein higher order structural analysis
    • Li CH, Nguyen X, Narhi L, Chemmalil L, Towers E, Muzammil S, Gabrielson J, Jiang Y. 2011. Applications of circular dichroism (CD) for structural analysis of proteins: Qualification of near- and far-UV CD for protein higher order structural analysis. J Pharm Sci 100(11):4642-4654.
    • (2011) J Pharm Sci , vol.100 , Issue.11 , pp. 4642-4654
    • Li, C.H.1    Nguyen, X.2    Narhi, L.3    Chemmalil, L.4    Towers, E.5    Muzammil, S.6    Gabrielson, J.7    Jiang, Y.8


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