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Volumn 154, Issue 1, 2011, Pages 27-34

A new method to increase selectivity of transglutaminase mediated PEGylation of salmon calcitonin and human growth hormone

Author keywords

Bio catalysis; Drug delivery; PEGylation; Protein modification; Therapeutic proteins

Indexed keywords

ALTERNATIVE METHODS; BIO-CATALYSIS; CHEMICAL PROCEDURES; COSOLVENTS; HUMAN GROWTH HORMONE; IN-VIVO; MICROBIAL TRANSGLUTAMINASE (MTGASE); PEGYLATION; PHARMACOLOGICAL PROPERTIES; PROTEIN MODIFICATION; REACTION MIXTURE; SALMON CALCITONIN; SECONDARY STRUCTURES; SITE-SELECTIVE CONJUGATION; SUBSTRATE PROTEINS; THERAPEUTIC PROTEIN; TRANSGLUTAMINASES;

EID: 79960925703     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2011.04.024     Document Type: Article
Times cited : (70)

References (41)
  • 1
    • 0037362655 scopus 로고    scopus 로고
    • Effect of pegylation on pharmaceuticals
    • DOI 10.1038/nrd1033
    • J.M. Harris, R.B. Chess, Effect of PEGylation on pharmaceuticals, Nat. Rev. Drug Discov. 2 (2003) 214-221. (Pubitemid 37361666)
    • (2003) Nature Reviews Drug Discovery , vol.2 , Issue.3 , pp. 214-221
    • Milton, H.J.1    Chess, R.B.2
  • 2
    • 34547607522 scopus 로고    scopus 로고
    • Polymer-drug conjugation, recent achievements and general strategies
    • G. Pasut, F.M. Veronese, Polymer-drug conjugation, recent achievements and general strategies, Prog. Polym. Sci. 32 (2007) 933-961.
    • (2007) Prog. Polym. Sci. , vol.32 , pp. 933-961
    • Pasut, G.1    Veronese, F.M.2
  • 3
    • 51549092094 scopus 로고    scopus 로고
    • The impact of PEGylation on biological therapies
    • A. Mero, F.M. Veronese, The impact of PEGylation on biological therapies, BioDrugs 22 (2008) 315-329.
    • (2008) BioDrugs , vol.22 , pp. 315-329
    • Mero, A.1    Veronese, F.M.2
  • 4
    • 26944452043 scopus 로고    scopus 로고
    • PEGylation, successful approach to drug delivery
    • DOI 10.1016/S1359-6446(05)03575-0, PII S1359644605035750
    • F.M. Veronese, G. Pasut, PEGylation, successful approach to drug delivery, Drug Discov. Today 10 (2005) 1451-1458. (Pubitemid 41483874)
    • (2005) Drug Discovery Today , vol.10 , Issue.21 , pp. 1451-1458
    • Veronese, F.M.1    Pasut, G.2
  • 5
    • 0042999388 scopus 로고    scopus 로고
    • Pegaspergase: A review of clinical studies
    • L.M. Graham, Pegaspergase: a review of clinical studies, Adv. Drug Deliv. Rev. 55 (2003) 1293-1302.
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 1293-1302
    • Graham, L.M.1
  • 6
    • 0023813205 scopus 로고
    • Adenosine deaminase deficiency with late onset of recurrent infections: Response to treatment with polyethylene glycol-modified adenosine deaminase
    • Y. Levy, M.S. Hershfield, C. Fernandez-Mejia, Adenosine deaminase deficiency with late onset of recurrent infections: response to treatment with polyethylene glycol-modified adenosine deaminase, J. Pediatr. 113 (1988) 312-317.
    • (1988) J. Pediatr. , vol.113 , pp. 312-317
    • Levy, Y.1    Hershfield, M.S.2    Fernandez-Mejia, C.3
  • 7
    • 0037124506 scopus 로고    scopus 로고
    • Chemistry for peptide and protein PEGylation
    • DOI 10.1016/S0169-409X(02)00022-4, PII S0169409X02000224
    • M.J. Roberts, M.D. Bentley, J.M. Harris, Chemistry for peptide and protein PEGylation, Adv. Drug Deliv. Rev. 54 (2002) 459-476. (Pubitemid 34615543)
    • (2002) Advanced Drug Delivery Reviews , vol.54 , Issue.4 , pp. 459-476
    • Roberts, M.J.1    Bentley, M.D.2    Harris, J.M.3
  • 8
    • 27844515221 scopus 로고    scopus 로고
    • PEG-proteins: Reaction engineering and separation issues
    • C.J. Fee, J.M. Van Alstine, PEG-proteins: reaction engineering and separation issues, Chem. Eng. Sci. 61 (2006) 924-939.
    • (2006) Chem. Eng. Sci. , vol.61 , pp. 924-939
    • Fee, C.J.1    Van Alstine, J.M.2
  • 9
    • 0037124398 scopus 로고    scopus 로고
    • Structural and biological characterization of pegylated recombinant interferon alpha-2b and its therapeutic implications
    • DOI 10.1016/S0169-409X(02)00027-3, PII S0169409X02000273
    • Y.S. Wang, S. Youngster, M. Grace, Structural and biological characterization of PEGylated recombinant interferon alpha-2b and its therapeutic implications, Adv. Drug Deliv. Rev. 54 (2002) 547-570. (Pubitemid 34618512)
    • (2002) Advanced Drug Delivery Reviews , vol.54 , Issue.4 , pp. 547-570
    • Wang, Y.-S.1    Youngster, S.2    Grace, M.3    Bausch, J.4    Bordens, R.5    Wyss, D.F.6
  • 12
    • 0029759584 scopus 로고    scopus 로고
    • Characterization and stability of N-terminally PEGylated rhG-CSF
    • O.B. Kinstler, D.N. Brems, S.L. Lauren, Characterization and stability of N-terminally PEGylated rhG-CSF, Pharm. Res. 13 (1996) 996-1002.
    • (1996) Pharm. Res. , vol.13 , pp. 996-1002
    • Kinstler, O.B.1    Brems, D.N.2    Lauren, S.L.3
  • 14
    • 34250200074 scopus 로고    scopus 로고
    • Identification and insertion of 3-carbon bridges in protein disulfide bonds: A computational approach
    • M. Zloh, S. Shaunak, S. Balan, S. Brocchini, Identification and insertion of 3-carbon bridges in protein disulfide bonds: a computational approach, Nat. Protoc. 2 (2007) 1070-1083.
    • (2007) Nat. Protoc. , vol.2 , pp. 1070-1083
    • Zloh, M.1    Shaunak, S.2    Balan, S.3    Brocchini, S.4
  • 15
    • 0037124507 scopus 로고    scopus 로고
    • Enzymatic procedure for site-specific PEGylation
    • H. Sato, Enzymatic procedure for site-specific PEGylation, Adv. Drug Deliv. Rev. 54 (2002) 487-504.
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 487-504
    • Sato, H.1
  • 16
    • 0028322985 scopus 로고
    • Transglutaminases: Protein cross-linking enzymes in tissues and body fluids
    • D. Aeschlimann, M. Paulsson, Transglutaminases: protein cross-linking enzymes in tissues and body fluids, Thromb. Haemost. 71 (1994) 402-415.
    • (1994) Thromb. Haemost. , vol.71 , pp. 402-415
    • Aeschlimann, D.1    Paulsson, M.2
  • 17
    • 2442610049 scopus 로고    scopus 로고
    • Properties and applications of microbial transglutaminase
    • DOI 10.1007/s00253-003-1539-5
    • K. Yokoyama, N. Nio, Y. Kikuchi, Properties and applications of microbial transglutaminase, Appl. Microbiol. Biotechnol. 64 (2004) 447-454. (Pubitemid 38686152)
    • (2004) Applied Microbiology and Biotechnology , vol.64 , Issue.4 , pp. 447-454
    • Yokoyama, K.1    Nio, N.2    Kikuchi, Y.3
  • 18
    • 62549119508 scopus 로고    scopus 로고
    • Transglutaminase-mediated-PEGylation of proteins: Direct identification of the sites of protein modification by mass spectrometry using a novel monodisperse PEG
    • A.Mero,B. Spolaore, F.M.Veronese,A. Fontana, Transglutaminase-mediated- PEGylation of proteins: direct identification of the sites of protein modification by mass spectrometry using a novel monodisperse PEG, Bioconjug. Chem. 20 (2009) 384-389.
    • (2009) Bioconjug. Chem. , vol.20 , pp. 384-389
    • Mero, A.1    Spolaore, B.2    Veronese, F.M.3    Fontana, A.4
  • 19
    • 36549039553 scopus 로고    scopus 로고
    • Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase
    • A. Fontana, B. Spolaore, A. Mero, F.M. Veronese, Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase, Adv. Drug Deliv. Rev. 60 (2008) 13-28.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 13-28
    • Fontana, A.1    Spolaore, B.2    Mero, A.3    Veronese, F.M.4
  • 20
    • 77949342622 scopus 로고    scopus 로고
    • A novel high-throughput screening method for microbial transglutaminases with high specificity toward Gln141 of human growth hormone
    • X. Zhao, A.C. Shaw, J. Wang, C.C. Chang, J. Deng, J. Su, A novel high-throughput screening method for microbial transglutaminases with high specificity toward Gln141 of human growth hormone, J. Biomol. Screen. 15 (2010) 206-212.
    • (2010) J. Biomol. Screen. , vol.15 , pp. 206-212
    • Zhao, X.1    Shaw, A.C.2    Wang, J.3    Chang, C.C.4    Deng, J.5    Su, J.6
  • 21
    • 77951884627 scopus 로고    scopus 로고
    • Transglutaminase-mediated methods for site-selective modification of human growth hormone
    • J. Buchardt, H. Selvig, P.F. Nielsen, J.N. Langeland, Transglutaminase-mediated methods for site-selective modification of human growth hormone, Pep. Sci. 94 (2010) 229-235.
    • (2010) Pep. Sci. , vol.94 , pp. 229-235
    • Buchardt, J.1    Selvig, H.2    Nielsen, P.F.3    Langeland, J.N.4
  • 22
    • 20044383430 scopus 로고    scopus 로고
    • Non-native intermediate conformational states of human growth hormone in the presence of organic solvents
    • M. Sukumar, S.M. Storms, M.R. De Felippis, Non-native intermediate conformational states of human growth hormone in the presence of organic solvents, Pharm. Res. 22 (2005) 789-796.
    • (2005) Pharm. Res. , vol.22 , pp. 789-796
    • Sukumar, M.1    Storms, S.M.2    De Felippis, M.R.3
  • 23
    • 0027523455 scopus 로고
    • Comparative study of human and salmon calcitonin secondary structure in solutions with low dielectric constants
    • T. Arvinte, A.F. Drake, Comparative study of human and salmon calcitonin secondary structure in solutions with low dielectric constants, J. Biol. Chem. 268 (1993) 6408-6414.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6408-6414
    • Arvinte, T.1    Drake, A.F.2
  • 25
    • 58149180219 scopus 로고    scopus 로고
    • Growth hormone therapy in children and adolescents: Pharmacokinetic/ pharmacodynamic considerations and emerging indications
    • L.A. Denson, Growth hormone therapy in children and adolescents: pharmacokinetic/pharmacodynamic considerations and emerging indications, Expert Opin. Drug Metab. Toxicol. 4 (2008) 1569-1580.
    • (2008) Expert Opin. Drug Metab. Toxicol. , vol.4 , pp. 1569-1580
    • Denson, L.A.1
  • 28
    • 33748151944 scopus 로고    scopus 로고
    • 18-amine specific PEGylation: Stability, permeability, pharmacokinetic behavior and in vivo hypocalcemic efficacy
    • DOI 10.1016/j.jconrel.2006.06.007, PII S016836590600280X
    • Y.S. Youn, J.Y. Jung, S.H. Oh, S.D. Yoo, K.C. Lee, Improved intestinal delivery of salmon calcitonin by Lys18-amine specific PEGylation: stability, permeability, pharmacokinetic behaviour and in vivo hypocalcaemic efficacy, J. Control. Release 114 (2006) 334-342. (Pubitemid 44310815)
    • (2006) Journal of Controlled Release , vol.114 , Issue.3 , pp. 334-342
    • Youn, Y.S.1    Jung, J.Y.2    Oh, S.H.3    Yoo, S.D.4    Lee, K.C.5
  • 29
    • 61649092532 scopus 로고    scopus 로고
    • Conjugation of salmon calcitonin to a combed-shaped end functionalized poly (poly(ethylene glycol) methyl ether methacrylate) yields a bioactive stable conjugate
    • S.M. Ryan, X. Wang, G. Mantovano, C.T. Sayers, D.M. Haddleton, D.J. Brayden, Conjugation of salmon calcitonin to a combed-shaped end functionalized poly (poly(ethylene glycol) methyl ether methacrylate) yields a bioactive stable conjugate, J. Control. Release 135 (2009) 51-59.
    • (2009) J. Control. Release , vol.135 , pp. 51-59
    • Ryan, S.M.1    Wang, X.2    Mantovano, G.3    Sayers, C.T.4    Haddleton, D.M.5    Brayden, D.J.6
  • 30
    • 76549212824 scopus 로고
    • The enzymatic formation of hydroxamic acids from glutamine and asparagines
    • N. Grossowicz, E. Wainfan, E. Borek, H. Waelsch, The enzymatic formation of hydroxamic acids from glutamine and asparagines, J. Biol. Chem. 187 (1950) 111-125.
    • (1950) J. Biol. Chem. , vol.187 , pp. 111-125
    • Grossowicz, N.1    Wainfan, E.2    Borek, E.3    Waelsch, H.4
  • 31
    • 46849096054 scopus 로고    scopus 로고
    • Stability and conformational changes of transglutaminase from Streptomyces hygroscopicus in ethanol-aqueous medium
    • L. Cui, G. Du, D. Zhang, X. Fan, J. Chen, Stability and conformational changes of transglutaminase from Streptomyces hygroscopicus in ethanol-aqueous medium, Process Biochem. 43 (2008) 887-891.
    • (2008) Process Biochem. , vol.43 , pp. 887-891
    • Cui, L.1    Du, G.2    Zhang, D.3    Fan, X.4    Chen, J.5
  • 32
    • 1842426531 scopus 로고    scopus 로고
    • Effects of polyethylene glycol on stability of a-chymotrypsin in aqueous ethanol solvent
    • DOI 10.1016/j.bbrc.2004.03.087, PII S0006291X04005807
    • L.M. Simon, M. Kotorman, A. Szabo, G. Garab, I. Laczko, Effects of polyethylene glycol on stability of a-chymotrypsin in aqueous ethanol solvent, Biochem. Biophys. Res. Commun. 317 (2004) 610-613. (Pubitemid 38452526)
    • (2004) Biochemical and Biophysical Research Communications , vol.317 , Issue.2 , pp. 610-613
    • Simon, L.M.1    Kotorman, M.2    Szabo, A.3    Garab, G.4    Laczko, I.5
  • 33
    • 33846251560 scopus 로고    scopus 로고
    • Effects of water-miscible solvents and polyhydroxy compounds on the structure and enzymatic activity of thermolysin
    • DOI 10.1016/j.jbiotec.2006.05.017, PII S0168165606004731
    • M. Pazhang, K. Khajeh, B. Ranjbar, S. Hosseinkhani, Effects of water-miscible solvents and polyhydroxy compounds on the structure and enzymatic activity of thermolysin, J. Biotechnol. 127 (2006) 45-53. (Pubitemid 46107118)
    • (2006) Journal of Biotechnology , vol.127 , Issue.1 , pp. 45-53
    • Pazhang, M.1    Khajeh, K.2    Ranjbar, B.3    Hosseinkhani, S.4
  • 35
    • 0024960675 scopus 로고
    • 1H NMR assignment and secondary structure determination of salmon calcitonin in solution
    • A. Motta, M.A. Castiglione-Morelli, N. Goud, P.A. Temessi, Sequential proton NMR assignment and secondary structure determination of salmon calcitonin in solution, Biochemistry 28 (1989) 7996-8002. (Pubitemid 19252879)
    • (1989) Biochemistry , vol.28 , Issue.20 , pp. 7996-8002
    • Motta, A.1    Castiglione, M.M.A.2    Goud, N.3    Temussi, P.A.4
  • 36
    • 0033038220 scopus 로고    scopus 로고
    • Conformational flexibility in calcitonin: The dynamic properties of human and salmon calcitonin in solution
    • DOI 10.1023/A:1008365322148
    • P. Amodeo, A. Motta, G. Strazzullo, M.A. Castiglione-Morelli, Conformational flexibility in calcitonin: the dynamic properties of human and salmon calcitonin in solution, J. Biomol. NMR 13 (1999) 161-174. (Pubitemid 29089226)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.2 , pp. 161-174
    • Amodeo, P.1    Motta, A.2    Strazzullo, G.3    Castiglione, M.M.A.4
  • 37
    • 0034609586 scopus 로고    scopus 로고
    • Identification of the major positional isomer of pegylated interferon alpha-2b
    • Y.S. Wang, S. Youngster, J. Bausch, R. Zhang, C. McNemar, D.F. Wyss, Identification of the major positional isomer of pegylated interferon alpha-2b, Biochemistry 39 (2000) 10634-10640.
    • (2000) Biochemistry , vol.39 , pp. 10634-10640
    • Wang, Y.S.1    Youngster, S.2    Bausch, J.3    Zhang, R.4    McNemar, C.5    Wyss, D.F.6
  • 38
    • 0029833619 scopus 로고    scopus 로고
    • Determinants for calcitonin analog interaction with the calcitonin receptor, N-terminus and transmembrane-loop regions
    • S.D. Stroop, H. Nakamuta, R.E. Kuestner, E.E. Moore, R.M. Epand, Determinants for calcitonin analog interaction with the calcitonin receptor, N-terminus and transmembrane-loop regions, Endocrinology 137 (1999) 4752-4756.
    • (1999) Endocrinology , vol.137 , pp. 4752-4756
    • Stroop, S.D.1    Nakamuta, H.2    Kuestner, R.E.3    Moore, E.E.4    Epand, R.M.5
  • 39
    • 0033055121 scopus 로고    scopus 로고
    • Isolation, characterization, and stability of positional isomers of mono-PEGylated salmon calcitonins
    • DOI 10.1023/A:1018861616465
    • K.C. Lee, S.C. Moon, M.O. Park, J.T. Lee, D.H. Na, S.D. Yoo, H.S. Lee, P.P. DeLuca, Isolation, characterization, and stability of positional isomers of mono-PEGylated salmon calcitonins, Pharm. Res. 16 (1999) 813-818. (Pubitemid 29284190)
    • (1999) Pharmaceutical Research , vol.16 , Issue.6 , pp. 813-818
    • Lee, K.C.1    Moon, S.C.2    Park, M.O.3    Lee, J.T.4    Na, D.H.5    Yoo, S.D.6    Lee, H.S.7    DeLuca, P.P.8
  • 40
    • 33846874991 scopus 로고    scopus 로고
    • High-yield production of biologically active mono-PEGylated salmon calcitonin by site-specific PEGylation
    • DOI 10.1016/j.jconrel.2006.11.013, PII S0168365906006687
    • Y.S. Youn, D.H. Na, K.C. Lee, High-yield production of biologically active mono-PEGylated salmon calcitonin by site-specific PEGylation, J. Control. Release 117 (2007) 371-379. (Pubitemid 46217941)
    • (2007) Journal of Controlled Release , vol.117 , Issue.3 , pp. 371-379
    • Youn, Y.S.1    Na, D.H.2    Lee, K.C.3
  • 41
    • 36649019135 scopus 로고    scopus 로고
    • Improved intrapulmonary delivery of site-specific PEGylated salmon calcitonin: Optimization by PEG size selection
    • DOI 10.1016/j.jconrel.2007.10.008, PII S0168365907005627
    • Y.S. Youn, M.-J. Kwon, D.H. Na, S.Y. Chae, S. Lee, K.C. Lee, Improved intrapulmonary delivery of site-specific PEGylated salmon calcitonim: optimization by PEG size selection, J. Control. Release 125 (2008) 68-75. (Pubitemid 350198681)
    • (2008) Journal of Controlled Release , vol.125 , Issue.1 , pp. 68-75
    • Youn, Y.S.1    Kwon, M.J.2    Na, D.H.3    Chae, S.Y.4    Lee, S.5    Lee, K.C.6


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