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Volumn 11, Issue 4, 2014, Pages 1259-1272

Screening methods to identify indole derivatives that protect against reactive oxygen species induced tryptophan oxidation in proteins

Author keywords

5 hydroxy indole; 5 hydroxy tryptophan; antioxidants; monoclonal antibodies; protein oxidation; reactive oxygen species; tryptophan

Indexed keywords

ANTIOXIDANT; AROMATIC CARBOXYLIC ACID; HYDROGEN PEROXIDE; HYDROXYL GROUP; HYDROXYL RADICAL; IMMUNOGLOBULIN G1 ANTIBODY; INDOLE DERIVATIVE; KYNURENINE; METHIONINE; MONOCLONAL ANTIBODY; REACTIVE OXYGEN METABOLITE; SINGLET OXYGEN; TRYPTOPHAN; TRYPTOPHAN DERIVATIVE;

EID: 84897992917     PISSN: 15438384     EISSN: 15438392     Source Type: Journal    
DOI: 10.1021/mp4007375     Document Type: Article
Times cited : (30)

References (46)
  • 1
    • 0029637161 scopus 로고
    • Chemical instability of protein pharmaceuticals: Mechanisms of oxidation and strategies for stabilization
    • Li, S.; Schöneich, C.; Borchardt, R. T. Chemical instability of protein pharmaceuticals: mechanisms of oxidation and strategies for stabilization Biotechnol. Bioeng. 1995, 48, 490-500
    • (1995) Biotechnol. Bioeng. , vol.48 , pp. 490-500
    • Li, S.1    Schöneich, C.2    Borchardt, R.T.3
  • 2
    • 34247125652 scopus 로고    scopus 로고
    • Identification of a single tryptophan residue as critical for binding activitiy in a humanized monoclonal antibody against respiratory syncytial virus
    • Wei, Z. Identification of a single tryptophan residue as critical for binding activitiy in a humanized monoclonal antibody against respiratory syncytial virus Anal. Chem. 2007, 79 (7) 2797-2805
    • (2007) Anal. Chem. , vol.79 , Issue.7 , pp. 2797-2805
    • Wei, Z.1
  • 3
    • 71649111656 scopus 로고    scopus 로고
    • Methionine, tryptophan, and histidine oxidation in a model protein, PTH: Mechanisms and stabilization
    • Ji, J. A. Methionine, tryptophan, and histidine oxidation in a model protein, PTH: mechanisms and stabilization J. Pharm. Sci. 2009, 98 (12) 4485-500
    • (2009) J. Pharm. Sci. , vol.98 , Issue.12 , pp. 4485-4500
    • Ji, J.A.1
  • 4
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: A formulation challenge
    • Frokjaer, S.; Otzen, D. E. Protein drug stability: a formulation challenge Nat. Rev. Drug Discovery 2005, 4 (4) 298-306
    • (2005) Nat. Rev. Drug Discovery , vol.4 , Issue.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 5
    • 37149012352 scopus 로고    scopus 로고
    • Fenton chemistry in biology and medicine
    • Prousek, J. Fenton chemistry in biology and medicine Pure Appl. Chem. 2007, 79 (12) 2325-2338
    • (2007) Pure Appl. Chem. , vol.79 , Issue.12 , pp. 2325-2338
    • Prousek, J.1
  • 6
    • 79958838317 scopus 로고    scopus 로고
    • Analysis of 2,2′-azobis (2-amidinopropane) dihydrochloride degradation and hydrolysis in aqueous solutions
    • Werber, J. Analysis of 2,2′-azobis (2-amidinopropane) dihydrochloride degradation and hydrolysis in aqueous solutions J. Pharm. Sci. 2011, 100 (8) 3307-3315
    • (2011) J. Pharm. Sci. , vol.100 , Issue.8 , pp. 3307-3315
    • Werber, J.1
  • 7
    • 80054773616 scopus 로고    scopus 로고
    • Site-specific tryptophan oxidation induced by autocatalytic reaction of polysorbate 20 in protein formulation
    • Lam, X. M. Site-specific tryptophan oxidation induced by autocatalytic reaction of polysorbate 20 in protein formulation Pharm. Res. 2011, 28 (10) 2543-2555
    • (2011) Pharm. Res. , vol.28 , Issue.10 , pp. 2543-2555
    • Lam, X.M.1
  • 8
    • 0030449173 scopus 로고    scopus 로고
    • Methionine residues as endogenous antioxidants in proteins
    • Levine, R. L. Methionine residues as endogenous antioxidants in proteins Proc. Natl. Acad. Sci. U.S.A. 1996, 93 (26) 15036-15040
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , Issue.26 , pp. 15036-15040
    • Levine, R.L.1
  • 9
    • 79951552251 scopus 로고    scopus 로고
    • Impact of methionine oxidation in human IgG1 Fc on serum half-life of monoclonal antibodies
    • Wang, W. R. Impact of methionine oxidation in human IgG1 Fc on serum half-life of monoclonal antibodies Mol. Immunol. 2011, 48 (6-7) 860-866
    • (2011) Mol. Immunol. , vol.48 , Issue.67 , pp. 860-866
    • Wang, W.R.1
  • 10
    • 64149109989 scopus 로고    scopus 로고
    • Impact of methionine oxidation on the binding of human IgG1 to Fc Rn and Fc gamma receptors
    • Bertolotti-Ciarlet, A. Impact of methionine oxidation on the binding of human IgG1 to Fc Rn and Fc gamma receptors Mol. Immunol. 2009, 46 (8-9) 1878-1882
    • (2009) Mol. Immunol. , vol.46 , Issue.89 , pp. 1878-1882
    • Bertolotti-Ciarlet, A.1
  • 11
    • 0030724407 scopus 로고    scopus 로고
    • Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2
    • Lam, X. M.; Yang, J. Y.; Cleland, J. L. Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2 J. Pharm. Sci. 1997, 86 (11) 1250-1255
    • (1997) J. Pharm. Sci. , vol.86 , Issue.11 , pp. 1250-1255
    • Lam, X.M.1    Yang, J.Y.2    Cleland, J.L.3
  • 12
    • 84989712905 scopus 로고
    • The photophysics and photochemistry of the near-UV absorbing amino-acids 0.1. Tryptophan and its simple derivatives
    • Creed, D. The photophysics and photochemistry of the near-UV absorbing amino-acids 0.1. Tryptophan and its simple derivatives Photochem. Photobiol. 1984, 39 (4) 537-562
    • (1984) Photochem. Photobiol. , vol.39 , Issue.4 , pp. 537-562
    • Creed, D.1
  • 13
    • 0026874055 scopus 로고
    • Tryptophan as an endogenous photosensitizer to elicit harmful effects of ultraviolet B
    • Babu, V.; Joshi, P. C. Tryptophan as an endogenous photosensitizer to elicit harmful effects of ultraviolet B Indian J. Biochem. Biophys. 1992, 29 (3) 296-298
    • (1992) Indian J. Biochem. Biophys. , vol.29 , Issue.3 , pp. 296-298
    • Babu, V.1    Joshi, P.C.2
  • 14
    • 0016851391 scopus 로고
    • Excited state chemistry of aromatic amino acids and related peptides
    • Bent, D. V.; Hayon, E. Excited state chemistry of aromatic amino acids and related peptides J. Am. Chem. Soc. 1975, 97 (10) 2612-2619
    • (1975) J. Am. Chem. Soc. , vol.97 , Issue.10 , pp. 2612-2619
    • Bent, D.V.1    Hayon, E.2
  • 15
    • 0017276638 scopus 로고
    • Characterization of a cell-lethal product from the photooxidation of tryptophan: Hydrogen peroxide
    • McCormick, J. P. Characterization of a cell-lethal product from the photooxidation of tryptophan: hydrogen peroxide Science 1976, 191 (4226) 468-469
    • (1976) Science , vol.191 , Issue.4226 , pp. 468-469
    • McCormick, J.P.1
  • 16
    • 0035823071 scopus 로고    scopus 로고
    • Antibody catalysis of the oxidation of water
    • Wentworth, P., Jr. Antibody catalysis of the oxidation of water Science 2001, 293 (5536) 1806-1811
    • (2001) Science , vol.293 , Issue.5536 , pp. 1806-1811
    • Wentworth Jr., P.1
  • 17
    • 0001672290 scopus 로고
    • Near-ultraviolet photooxidation of tryptophan - Proof of formation of superoxide ion
    • McCormick, J. P.; Thomason, T. Near-ultraviolet photooxidation of tryptophan-proof of formation of superoxide ion J. Am. Chem. Soc. 1978, 100, 312-313
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 312-313
    • McCormick, J.P.1    Thomason, T.2
  • 18
    • 0037564169 scopus 로고    scopus 로고
    • Singlet oxygen-mediated damage to proteins and its consequences
    • Davies, M. J. Singlet oxygen-mediated damage to proteins and its consequences Biochem. Biophys. Res. Commun. 2003, 305 (3) 761-770
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , Issue.3 , pp. 761-770
    • Davies, M.J.1
  • 19
    • 0027142171 scopus 로고
    • DNA breaking activity of the carbon-centered radical generated from 2,2′-azobis(2-amidinopropane) hydrochloride (AAPH)
    • Hiramoto, K. DNA breaking activity of the carbon-centered radical generated from 2,2′-azobis(2-amidinopropane) hydrochloride (AAPH) Free Radical Res. Commun. 1993, 19 (5) 323-332
    • (1993) Free Radical Res. Commun. , vol.19 , Issue.5 , pp. 323-332
    • Hiramoto, K.1
  • 20
    • 0030952676 scopus 로고    scopus 로고
    • Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems
    • Chao, C. C.; Ma, Y. S.; Stadtman, E. R. Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems Proc. Natl. Acad. Sci. U.S.A. 1997, 94 (7) 2969-2974
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , Issue.7 , pp. 2969-2974
    • Chao, C.C.1    Ma, Y.S.2    Stadtman, E.R.3
  • 21
    • 34250781639 scopus 로고    scopus 로고
    • Protect from light: Photodegradation and protein biologics
    • Kerwin, B. A.; Remmele, R. L., Jr. Protect from light: photodegradation and protein biologics J. Pharm. Sci. 2007, 96 (6) 1468-1479
    • (2007) J. Pharm. Sci. , vol.96 , Issue.6 , pp. 1468-1479
    • Kerwin, B.A.1    Remmele Jr., R.L.2
  • 22
    • 84859892575 scopus 로고
    • Quality of Biotechnological Products: Stability Testing of Biotechnological/Biological Products
    • In; ICH: Geneva, Switzerland.
    • Quality of Biotechnological Products: Stability Testing of Biotechnological/Biological Products. In International Conference on Harmonisation 1995; ICH: Geneva, Switzerland, 1995.
    • (1995) International Conference on Harmonisation 1995
  • 23
    • 33646068727 scopus 로고    scopus 로고
    • Screening methods for antioxidants-A review
    • Kaur, I. P.; Geetha, T. Screening methods for antioxidants-a review Mini Rev. Med. Chem. 2006, 6 (3) 305-312
    • (2006) Mini Rev. Med. Chem. , vol.6 , Issue.3 , pp. 305-312
    • Kaur, I.P.1    Geetha, T.2
  • 24
    • 78649828698 scopus 로고    scopus 로고
    • Analysis of the antioxidant activity of an indole library: Cyclic voltammetry versus ROS scavenging activity
    • Estevao, M. S. Analysis of the antioxidant activity of an indole library: cyclic voltammetry versus ROS scavenging activity Tetrahedron Lett. 2011, 52 (1) 101-106
    • (2011) Tetrahedron Lett. , vol.52 , Issue.1 , pp. 101-106
    • Estevao, M.S.1
  • 25
    • 0036395858 scopus 로고    scopus 로고
    • Stabilization of pharmaceuticals to oxidative degradation
    • Waterman, K. C. Stabilization of pharmaceuticals to oxidative degradation Pharm. Dev. Technol. 2002, 7 (1) 1-32
    • (2002) Pharm. Dev. Technol. , vol.7 , Issue.1 , pp. 1-32
    • Waterman, K.C.1
  • 26
    • 0035425177 scopus 로고    scopus 로고
    • Engineering and design in the bioelectrochemistry of metalloproteins
    • Gilardi, G.; Fantuzzi, A.; Sadeghi, S. J. Engineering and design in the bioelectrochemistry of metalloproteins Curr. Opin. Struct. Biol. 2001, 11 (4) 491-499
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , Issue.4 , pp. 491-499
    • Gilardi, G.1    Fantuzzi, A.2    Sadeghi, S.J.3
  • 27
    • 33645057962 scopus 로고    scopus 로고
    • Rapid screening of antioxidants in pharmaceutical formulation development using cyclic voltammetry - Potential and limitations
    • Huang, T.; Gao, P.; Hageman, M. J. Rapid screening of antioxidants in pharmaceutical formulation development using cyclic voltammetry - potential and limitations Curr. Drug Discovery Technol. 2004, 1 (2) 173-179
    • (2004) Curr. Drug Discovery Technol. , vol.1 , Issue.2 , pp. 173-179
    • Huang, T.1    Gao, P.2    Hageman, M.J.3
  • 28
    • 34848924103 scopus 로고    scopus 로고
    • Photoreactivity of amino acids: Tryptophan-induced photochemical events via reactive oxygen species generation
    • Igarashi, N.; Onoue, S.; Tsuda, Y. Photoreactivity of amino acids: tryptophan-induced photochemical events via reactive oxygen species generation Anal. Sci. 2007, 23 (8) 943-948
    • (2007) Anal. Sci. , vol.23 , Issue.8 , pp. 943-948
    • Igarashi, N.1    Onoue, S.2    Tsuda, Y.3
  • 29
    • 84872140390 scopus 로고    scopus 로고
    • Role of surface exposed tryptophan in the antibody catalyzed water oxidation pathway
    • Sreedhara, A. Role of surface exposed tryptophan in the antibody catalyzed water oxidation pathway Mol. Pharmaceutics 2013, 10, 278-288
    • (2013) Mol. Pharmaceutics , vol.10 , pp. 278-288
    • Sreedhara, A.1
  • 30
    • 0034718510 scopus 로고    scopus 로고
    • Antibodies have the intrinsic capacity to destroy antigens
    • Wentworth, A. D. Antibodies have the intrinsic capacity to destroy antigens Proc. Natl. Acad. Sci. U.S.A. 2000, 97 (20) 10930-10935
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , Issue.20 , pp. 10930-10935
    • Wentworth, A.D.1
  • 31
    • 1442306216 scopus 로고    scopus 로고
    • Probing the antibody-catalyzed water-oxidation pathway at atomic resolution
    • Zhu, X. Probing the antibody-catalyzed water-oxidation pathway at atomic resolution Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (8) 2247-2252
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.8 , pp. 2247-2252
    • Zhu, X.1
  • 32
    • 77949265999 scopus 로고    scopus 로고
    • Oxidation of Free L-histidine by tert-Butylhydroperoxide
    • Mason, B. D. Oxidation of Free L-histidine by tert-Butylhydroperoxide Pharm. Res. 2010, 27 (3) 447-456
    • (2010) Pharm. Res. , vol.27 , Issue.3 , pp. 447-456
    • Mason, B.D.1
  • 33
    • 0028391073 scopus 로고
    • Reactivity of Singlet Oxygen toward Amino-Acids and Peptides
    • Michaeli, A.; Feitelson, J. Reactivity of Singlet Oxygen toward Amino-Acids and Peptides Photochem. Photobiol. 1994, 59 (3) 284-289
    • (1994) Photochem. Photobiol. , vol.59 , Issue.3 , pp. 284-289
    • Michaeli, A.1    Feitelson, J.2
  • 34
    • 49649130587 scopus 로고
    • Role of azide in singlet oxygen reactions: Reaction of azide with singlet oxygen
    • Hasty, N. Role of azide in singlet oxygen reactions: Reaction of azide with singlet oxygen Tetrahedron Lett. 1972, 49-52
    • (1972) Tetrahedron Lett. , pp. 49-52
    • Hasty, N.1
  • 35
    • 79959996651 scopus 로고    scopus 로고
    • Antioxidant properties and associated mechanisms of salicylates
    • Baltazar, M. T. Antioxidant properties and associated mechanisms of salicylates Curr. Med. Chem. 2011, 18 (21) 3252-3264
    • (2011) Curr. Med. Chem. , vol.18 , Issue.21 , pp. 3252-3264
    • Baltazar, M.T.1
  • 36
    • 0027201993 scopus 로고
    • The pineal hormone melatonin inhibits DNA-adduct formation induced by the chemical carcinogen safrole in-vivo
    • Tan, D. X. The pineal hormone melatonin inhibits DNA-adduct formation induced by the chemical carcinogen safrole in-vivo Cancer Lett 1993, 70 (1-2) 65-71
    • (1993) Cancer Lett , vol.70 , Issue.12 , pp. 65-71
    • Tan, D.X.1
  • 37
    • 0030986012 scopus 로고    scopus 로고
    • Reaction of melatonin and related indoles with hydroxyl radicals: EPR and spin trapping investigations
    • Matuszak, Z.; Reszka, K.; Chignell, C. F. Reaction of melatonin and related indoles with hydroxyl radicals: EPR and spin trapping investigations Free Radical Biol. Med. 1997, 23 (3) 367-372
    • (1997) Free Radical Biol. Med. , vol.23 , Issue.3 , pp. 367-372
    • Matuszak, Z.1    Reszka, K.2    Chignell, C.F.3
  • 38
    • 0027429994 scopus 로고
    • The significance of the metabolism of the neurohormone melatonin: Antioxidative protection and formation of bioactive substances
    • Hardeland, R. The significance of the metabolism of the neurohormone melatonin: antioxidative protection and formation of bioactive substances Neurosci. Biobehav. Rev. 1993, 17 (3) 347-357
    • (1993) Neurosci. Biobehav. Rev. , vol.17 , Issue.3 , pp. 347-357
    • Hardeland, R.1
  • 39
    • 58549108963 scopus 로고    scopus 로고
    • Protective effect of melatonin on photo-damage to lysozyme
    • Zhu, H. Protective effect of melatonin on photo-damage to lysozyme J. Photochem. Photobiol., B 2009, 94 (2) 125-130
    • (2009) J. Photochem. Photobiol., B , vol.94 , Issue.2 , pp. 125-130
    • Zhu, H.1
  • 40
    • 12344305096 scopus 로고    scopus 로고
    • 5-hydroxytryptophan is a more potent in vitro hydroxyl radical scavenger than melatonin or vitamin C
    • Keithahn, C.; Lerchl, A. 5-hydroxytryptophan is a more potent in vitro hydroxyl radical scavenger than melatonin or vitamin C J. Pineal Res. 2005, 38 (1) 62-66
    • (2005) J. Pineal Res. , vol.38 , Issue.1 , pp. 62-66
    • Keithahn, C.1    Lerchl, A.2
  • 41
    • 77952629492 scopus 로고    scopus 로고
    • 5-Hydroxytrytophan inhibits tert-butylhydroperoxide (t-BHP)-induced oxidative damage via the suppression of reactive species (RS) and nuclear factor-kappaB (NF-kappaB) activation on human fibroblast
    • Bae, S. J. 5-Hydroxytrytophan inhibits tert-butylhydroperoxide (t-BHP)-induced oxidative damage via the suppression of reactive species (RS) and nuclear factor-kappaB (NF-kappaB) activation on human fibroblast J. Agric. Food Chem. 2010, 58 (10) 6387-6394
    • (2010) J. Agric. Food Chem. , vol.58 , Issue.10 , pp. 6387-6394
    • Bae, S.J.1
  • 42
    • 0000766427 scopus 로고    scopus 로고
    • Photosensitized generation of singlet oxygen from vinyl linked benzo-crown-ether-bipyridyl ruthenium(II) complexes
    • Abdel-Shafi, A. A. Photosensitized generation of singlet oxygen from vinyl linked benzo-crown-ether-bipyridyl ruthenium(II) complexes J. Phys. Chem. A 2000, 104 (2) 192-202
    • (2000) J. Phys. Chem. A , vol.104 , Issue.2 , pp. 192-202
    • Abdel-Shafi, A.A.1
  • 43
    • 0000512549 scopus 로고    scopus 로고
    • Mechanism of quenching of triplet states by molecular oxygen: Biphenyl derivatives in different solvents
    • Wilkinson, F.; Abdel-Shafi, A. A. Mechanism of quenching of triplet states by molecular oxygen: Biphenyl derivatives in different solvents J. Phys. Chem. A 1999, 103 (28) 5425-5435
    • (1999) J. Phys. Chem. A , vol.103 , Issue.28 , pp. 5425-5435
    • Wilkinson, F.1    Abdel-Shafi, A.A.2
  • 44
    • 13544265606 scopus 로고    scopus 로고
    • Identification and reactivity of the triplet excited state of 5-hydroxytryptophan
    • Dad, S. Identification and reactivity of the triplet excited state of 5-hydroxytryptophan J. Photochem. Photobiol., B 2005, 78 (3) 245-251
    • (2005) J. Photochem. Photobiol., B , vol.78 , Issue.3 , pp. 245-251
    • Dad, S.1
  • 45
    • 7744239249 scopus 로고
    • Further comments on the redox potentials of tryptophan and tyrosine
    • Harriman, A. Further comments on the redox potentials of tryptophan and tyrosine J. Phys. Chem. 1987, 91 (24) 6102-6104
    • (1987) J. Phys. Chem. , vol.91 , Issue.24 , pp. 6102-6104
    • Harriman, A.1
  • 46
    • 0347285302 scopus 로고    scopus 로고
    • Sanguinarine is a potent inhibitor of oxidative burst in DMSO-differentiated HL-60 cells by a non-redox mechanism
    • Vrba, J. Sanguinarine is a potent inhibitor of oxidative burst in DMSO-differentiated HL-60 cells by a non-redox mechanism Chem.-Biol. Interact. 2004, 147 (1) 35-47
    • (2004) Chem.-Biol. Interact. , vol.147 , Issue.1 , pp. 35-47
    • Vrba, J.1


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