메뉴 건너뛰기




Volumn 102, Issue 1, 2013, Pages 52-61

Application of second-derivative fluorescence spectroscopy to monitor subtle changes in a monoclonal antibody structure

Author keywords

Excipients; Fluorescence spectroscopy; Monoclonal antibodies; Polyols; Protein aggregation; Protein structure; Protein unfolding; Proteins; Second derivative; Tryptophan

Indexed keywords

BUFFER; ETHYLENE GLYCOL; MONOCLONAL ANTIBODY; POLYOL; SUCROSE; TRYPTOPHAN; UREA;

EID: 84870709849     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23354     Document Type: Article
Times cited : (18)

References (33)
  • 1
    • 0344084062 scopus 로고    scopus 로고
    • Temperature- and pH-induced multiple partially unfolded states of recombinant human interferon- 2a: Possible implications in protein stability
    • Sharma VK, Kalonia DS. 2003. Temperature- and pH-induced multiple partially unfolded states of recombinant human interferon- 2a: Possible implications in protein stability. Pharm Res 20:1721-1729.
    • (2003) Pharm Res , vol.20 , pp. 1721-1729
    • Sharma, V.K.1    Kalonia, D.S.2
  • 2
    • 23444456924 scopus 로고    scopus 로고
    • How to study proteins by circular dichroism
    • Kelly S, Jess T, Price N. 2005. How to study proteins by circular dichroism. Biochim Biophys Acta 1751:119-139.
    • (2005) Biochim Biophys Acta , vol.1751 , pp. 119-139
    • Kelly, S.1    Jess, T.2    Price, N.3
  • 3
    • 0041336626 scopus 로고    scopus 로고
    • Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: A bGCSF case study
    • Kueltzo LA, Ersoy B, Ralston JP, Middaugh CR. 2003. Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: A bGCSF case study. J Pharm Sci 92:1805-1820.
    • (2003) J Pharm Sci , vol.92 , pp. 1805-1820
    • Kueltzo, L.A.1    Ersoy, B.2    Ralston, J.P.3    Middaugh, C.R.4
  • 4
    • 33646918845 scopus 로고    scopus 로고
    • Probing protein folding and conformational transitions with fluorescence
    • Royer CA. 2006. Probing protein folding and conformational transitions with fluorescence. Chem Rev 106:1769-1784.
    • (2006) Chem Rev , vol.106 , pp. 1769-1784
    • Royer, C.A.1
  • 5
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein EA, Vedenkina NS, Ivkova MN. 1973. Fluorescence and the location of tryptophan residues in protein molecules. Photochem Photobiol 18:263-279.
    • (1973) Photochem Photobiol , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 6
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink MR. 1994. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys J 66:482-501.
    • (1994) Biophys J , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 9
    • 44649133131 scopus 로고    scopus 로고
    • Extrinsic fluorescent dyes as tools for protein characterization
    • Hawe A, Sutter M, Jiskoot W. 2008. Extrinsic fluorescent dyes as tools for protein characterization. Pharm Res 25:1487-1499.
    • (2008) Pharm Res , vol.25 , pp. 1487-1499
    • Hawe, A.1    Sutter, M.2    Jiskoot, W.3
  • 10
    • 0014354873 scopus 로고
    • Fluorescence spectroscopy of proteins
    • Stryer L. 1968. Fluorescence spectroscopy of proteins. Science 162:526-533.
    • (1968) Science , vol.162 , pp. 526-533
    • Stryer, L.1
  • 11
    • 0141770516 scopus 로고
    • Derivative fluorescence spectroscopy
    • Miller JN, Ahmad TA, Fell AF. 1982. Derivative fluorescence spectroscopy. Anal Proc 19:37-41.
    • (1982) Anal Proc , vol.19 , pp. 37-41
    • Miller, J.N.1    Ahmad, T.A.2    Fell, A.F.3
  • 12
    • 0037016375 scopus 로고    scopus 로고
    • Second derivative fluorescence spectroscopy of tryptophan in proteins
    • Mozo-Villarias A. 2002. Second derivative fluorescence spectroscopy of tryptophan in proteins. J Biochem Biophys Methods 50:163-178.
    • (2002) J Biochem Biophys Methods , vol.50 , pp. 163-178
    • Mozo-Villarias, A.1
  • 13
    • 16244362365 scopus 로고    scopus 로고
    • Second derivative tryptophan fluorescence spectroscopy as a tool to characterize partially unfolded intermediates of proteins
    • Kumar V, Sharma VK, Kalonia DS. 2005. Second derivative tryptophan fluorescence spectroscopy as a tool to characterize partially unfolded intermediates of proteins. Int J Pharm 294:193-199.
    • (2005) Int J Pharm , vol.294 , pp. 193-199
    • Kumar, V.1    Sharma, V.K.2    Kalonia, D.S.3
  • 15
    • 0001943903 scopus 로고    scopus 로고
    • Fluorescence spectroscopy in peptide and protein analysis
    • Meyers RA, Ed. Chichester, England: John Wiley & Sons Ltd.
    • Ladokhin AS. 2000. Fluorescence spectroscopy in peptide and protein analysis. In Encyclopedia of analytical chemistry; Meyers RA, Ed. Chichester, England: John Wiley & Sons Ltd., pp 5762-5779.
    • (2000) Encyclopedia of analytical chemistry , pp. 5762-5779
    • Ladokhin, A.S.1
  • 17
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous solution
    • Szabo AG, Rayner DM. 1980. Fluorescence decay of tryptophan conformers in aqueous solution. J Am Chem Soc 102:554-563.
    • (1980) J Am Chem Soc , vol.102 , pp. 554-563
    • Szabo, A.G.1    Rayner, D.M.2
  • 21
    • 0039842514 scopus 로고    scopus 로고
    • Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer
    • Uhrinova S, Smith MH, Jameson GB, Uhrin D, Sawyer L, Barlow PN. 2000. Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer. Biochemistry 39:3565-3574.
    • (2000) Biochemistry , vol.39 , pp. 3565-3574
    • Uhrinova, S.1    Smith, M.H.2    Jameson, G.B.3    Uhrin, D.4    Sawyer, L.5    Barlow, P.N.6
  • 22
    • 34047265288 scopus 로고    scopus 로고
    • A tryptophan rotamer located in a polar environment probes pH-dependent conformational changes in bovine-lactoglobulin A
    • Harvey BJ, Bell E, Brancaleon L. 2007. A tryptophan rotamer located in a polar environment probes pH-dependent conformational changes in bovine-lactoglobulin A. J Phys Chem B 111:2610-2620.
    • (2007) J Phys Chem B , vol.111 , pp. 2610-2620
    • Harvey, B.J.1    Bell, E.2    Brancaleon, L.3
  • 23
    • 0031875535 scopus 로고    scopus 로고
    • Some aspects of β-lactoglobulin structural properties in solution studied by fluorescence quenching
    • Busti P, Gatti CA, Delorenzi NJ. 1998. Some aspects of β-lactoglobulin structural properties in solution studied by fluorescence quenching. Int J Biol Macromol 23:143-148.
    • (1998) Int J Biol Macromol , vol.23 , pp. 143-148
    • Busti, P.1    Gatti, C.A.2    Delorenzi, N.J.3
  • 24
    • 0032004945 scopus 로고    scopus 로고
    • Effects of pH and salt environment on the association of beta-lactoglobulin revealed by intrinsic fluorescence studies
    • Renard D, Lefebvre J, Griffin MCA, Griffin WG. 1998. Effects of pH and salt environment on the association of beta-lactoglobulin revealed by intrinsic fluorescence studies. Int J Biol Macromol 22:41-49.
    • (1998) Int J Biol Macromol , vol.22 , pp. 41-49
    • Renard, D.1    Lefebvre, J.2    Griffin, M.C.A.3    Griffin, W.G.4
  • 25
    • 33747488943 scopus 로고    scopus 로고
    • Formulation and delivery issues for monoclonal antibody therapeutics
    • Daugherty AL, Mrsny RJ. 2006. Formulation and delivery issues for monoclonal antibody therapeutics. Adv Drug Del Rev 58:686-706.
    • (2006) Adv Drug Del Rev , vol.58 , pp. 686-706
    • Daugherty, A.L.1    Mrsny, R.J.2
  • 26
    • 0018789680 scopus 로고
    • Increased thermal stability of proteins in the presence of sugars and polyols
    • Back JF, Oakenfull D, Smith MB. 1979. Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry 18:5191-5196.
    • (1979) Biochemistry , vol.18 , pp. 5191-5196
    • Back, J.F.1    Oakenfull, D.2    Smith, M.B.3
  • 27
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes
    • Timasheff SN. 1993. The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Ann Rev Biophys Biomol Struct 22:67-97.
    • (1993) Ann Rev Biophys Biomol Struct , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 28
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee JC, Timasheff SN. 1981. The stabilization of proteins by sucrose. J Biol Chem 256:7193-7201.
    • (1981) J Biol Chem , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 29
    • 23644438008 scopus 로고    scopus 로고
    • Effect of polyol osmolytes on ΔGD, the Gibbs energy of stabilisation of proteins at different pH values
    • Haque I, Singh R, Moosavi-Movahedi AA, Ahmad F. 2005. Effect of polyol osmolytes on ΔGD, the Gibbs energy of stabilisation of proteins at different pH values. Biophys Chem 117:1-12.
    • (2005) Biophys Chem , vol.117 , pp. 1-12
    • Haque, I.1    Singh, R.2    Moosavi-Movahedi, A.A.3    Ahmad, F.4
  • 31
    • 0030973690 scopus 로고    scopus 로고
    • The thermodynamic mechanism of protein stabilization by trehalose
    • Xie G, Timasheff SN. 1997. The thermodynamic mechanism of protein stabilization by trehalose. Biophys Chem 64:25-43.
    • (1997) Biophys Chem , vol.64 , pp. 25-43
    • Xie, G.1    Timasheff, S.N.2
  • 32
    • 0023505188 scopus 로고
    • Thermal stability of proteins in the presence of poly (ethylene glycols)
    • Lee L, Lee J. 1987. Thermal stability of proteins in the presence of poly (ethylene glycols). Biochemistry 26:7813-7819.
    • (1987) Biochemistry , vol.26 , pp. 7813-7819
    • Lee, L.1    Lee, J.2
  • 33
    • 0346982114 scopus 로고    scopus 로고
    • Challenges and issues in the development of formulations of protein pharmaceuticals
    • Wu-Pong S, Ronjanasakul Y, Eds. Totowa, New Jersey: Humana Press Inc.
    • Shire S. 1999. Challenges and issues in the development of formulations of protein pharmaceuticals. In Biopharmaceutical drug design and development; Wu-Pong S, Ronjanasakul Y, Eds. Totowa, New Jersey: Humana Press Inc., pp 205-238.
    • (1999) Biopharmaceutical drug design and development , pp. 205-238
    • Shire, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.