메뉴 건너뛰기




Volumn 53, Issue 8, 2009, Pages 3496-3500

Stability of peroxide antimalarials in the presence of human hemoglobin

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMALARIAL AGENT; ARTEMETHER; DIHYDROARTEMISININ; HEME; OXYHEMOGLOBIN; OZ 277; OZ 78; UNCLASSIFIED DRUG;

EID: 67749142076     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00363-09     Document Type: Article
Times cited : (23)

References (39)
  • 1
    • 0031059859 scopus 로고    scopus 로고
    • In-vitro interaction of artemisinin with intact human erythrocytes, erythrocyte ghosts, haemoglobin and carbonic anhydrase
    • Bakhshi, H. B., T. Gordi, and M. Ashton. 1997. In-vitro interaction of artemisinin with intact human erythrocytes, erythrocyte ghosts, haemoglobin and carbonic anhydrase. J. Pharm. Pharmacol. 49:223-226.
    • (1997) J. Pharm. Pharmacol , vol.49 , pp. 223-226
    • Bakhshi, H.B.1    Gordi, T.2    Ashton, M.3
  • 2
    • 0015843337 scopus 로고
    • Equations for the spectrophotometric analysis of hemoglobin mixtures
    • Benesch, R. E., R. Benesch, and S. Yung. 1973. Equations for the spectrophotometric analysis of hemoglobin mixtures. Anal. Biochem. 55:245-248.
    • (1973) Anal. Biochem , vol.55 , pp. 245-248
    • Benesch, R.E.1    Benesch, R.2    Yung, S.3
  • 3
    • 0029016290 scopus 로고
    • Coupled reactions in hemoglobin
    • Benesch, R. E., and S. Kwong. 1995. Coupled reactions in hemoglobin. J. Biol. Chem. 270:13785-13786.
    • (1995) J. Biol. Chem , vol.270 , pp. 13785-13786
    • Benesch, R.E.1    Kwong, S.2
  • 4
    • 42049102584 scopus 로고    scopus 로고
    • Creek, D. J., W. N. Charman, F. C. K. Chiu, R. J. Prankerd, Y. Dong, J. L. Vennerstrom, and S. A. Charman. 2008. Relationship between antimalarial activity and heme alkylation for spiro- and dispiro-1,2,4- trioxolane antimalarials. Antimicrob. Agents Chemother. 52:1291-1296.
    • Creek, D. J., W. N. Charman, F. C. K. Chiu, R. J. Prankerd, Y. Dong, J. L. Vennerstrom, and S. A. Charman. 2008. Relationship between antimalarial activity and heme alkylation for spiro- and dispiro-1,2,4- trioxolane antimalarials. Antimicrob. Agents Chemother. 52:1291-1296.
  • 5
    • 36149001570 scopus 로고    scopus 로고
    • Creek, D. J., W. N. Charman, F. C. K. Chiu, R. J. Prankerd, K. J. McCullough, Y. Dong, J. L. Vennerstrom, and S. A. Charman. 2007. Iron-mediated degradation kinetics of substituted dispiro-1,2,4-trioxolane antimalarials. J. Pharm. Sci. 96:2945-2956.
    • Creek, D. J., W. N. Charman, F. C. K. Chiu, R. J. Prankerd, K. J. McCullough, Y. Dong, J. L. Vennerstrom, and S. A. Charman. 2007. Iron-mediated degradation kinetics of substituted dispiro-1,2,4-trioxolane antimalarials. J. Pharm. Sci. 96:2945-2956.
  • 6
    • 25444475493 scopus 로고    scopus 로고
    • Creek, D. J., F. C. K. Chiu, R. J. Prankerd, S. A. Charman, and W. N. Charman. 2005. Kinetics of iron-mediated artemisinin degradation: effect of solvent composition and iron salt. J. Pharm. Sci. 94:1820-1829.
    • Creek, D. J., F. C. K. Chiu, R. J. Prankerd, S. A. Charman, and W. N. Charman. 2005. Kinetics of iron-mediated artemisinin degradation: effect of solvent composition and iron salt. J. Pharm. Sci. 94:1820-1829.
  • 7
    • 0019739893 scopus 로고
    • Preparation of derivatives of ferrous and ferric hemoglobin
    • Di Iorio, E. E. 1981. Preparation of derivatives of ferrous and ferric hemoglobin. Methods Enzymol 76:57-72.
    • (1981) Methods Enzymol , vol.76 , pp. 57-72
    • Di Iorio, E.E.1
  • 8
    • 0030879653 scopus 로고    scopus 로고
    • Hemoglobin metabolism in the malaria parasite Plasmodium falciparum
    • Francis, S. E., D. J. Sullivan, and D. E. Goldberg. 1997. Hemoglobin metabolism in the malaria parasite Plasmodium falciparum. Annu. Rev. Microbiol. 51:97-123.
    • (1997) Annu. Rev. Microbiol , vol.51 , pp. 97-123
    • Francis, S.E.1    Sullivan, D.J.2    Goldberg, D.E.3
  • 10
    • 0030814099 scopus 로고    scopus 로고
    • Quaternary structure regulates hemin dissociation from human hemoglobin
    • Hargrove, M. S., T. Whitaker, J. S. Olson, R. J. Vali, and A. J. Mathews. 1997. Quaternary structure regulates hemin dissociation from human hemoglobin. J. Biol. Chem. 272:17385-17389.
    • (1997) J. Biol. Chem , vol.272 , pp. 17385-17389
    • Hargrove, M.S.1    Whitaker, T.2    Olson, J.S.3    Vali, R.J.4    Mathews, A.J.5
  • 11
    • 0031898891 scopus 로고    scopus 로고
    • Alteration of redox stability of hemoglobins A and S by biological buffers
    • Harrington, J. P. 1998. Alteration of redox stability of hemoglobins A and S by biological buffers. Comp. Biochem. Physiol. B 119:305-309.
    • (1998) Comp. Biochem. Physiol. B , vol.119 , pp. 305-309
    • Harrington, J.P.1
  • 12
    • 0027241446 scopus 로고
    • Unfolding and release of heme from human hemoglobins A, S and F
    • Harrington, J. P., and L. Keaton. 1993. Unfolding and release of heme from human hemoglobins A, S and F. Int. J. Biochem. 25:661-664.
    • (1993) Int. J. Biochem , vol.25 , pp. 661-664
    • Harrington, J.P.1    Keaton, L.2
  • 13
    • 34249012765 scopus 로고    scopus 로고
    • New developments in synthetic peroxidic drugs as artemisinin mimics
    • Jefford, C. W. 2007. New developments in synthetic peroxidic drugs as artemisinin mimics. Drug Discov. Today 12:487-495.
    • (2007) Drug Discov. Today , vol.12 , pp. 487-495
    • Jefford, C.W.1
  • 14
    • 12844258876 scopus 로고    scopus 로고
    • Reaction of artemisinin with hemoglobin: Implications for antimalarial activity
    • Kannan, R., K. Kumar, D. Sahal, S. Kukreti, and V. S. Chauhan. 2004. Reaction of artemisinin with hemoglobin: implications for antimalarial activity. Biochem. J. 385:409-418.
    • (2004) Biochem. J , vol.385 , pp. 409-418
    • Kannan, R.1    Kumar, K.2    Sahal, D.3    Kukreti, S.4    Chauhan, V.S.5
  • 15
    • 33646582624 scopus 로고    scopus 로고
    • Re-evaluation of how artemisinins work in light of emerging evidence of in vitro resistance
    • Krishna, S., C. J. Woodrow, H. M. Staines, R. K. Haynes, and O. Mercereau-Puijalon. 2006. Re-evaluation of how artemisinins work in light of emerging evidence of in vitro resistance. Trends Mol. Med. 12:200-205.
    • (2006) Trends Mol. Med , vol.12 , pp. 200-205
    • Krishna, S.1    Woodrow, C.J.2    Staines, H.M.3    Haynes, R.K.4    Mercereau-Puijalon, O.5
  • 16
    • 0023932566 scopus 로고
    • Detection of hemin release during hemoglobin S denaturation
    • Liu, S. C., S. Zhai, and J. Palek. 1988. Detection of hemin release during hemoglobin S denaturation. Blood 71:1755-1758.
    • (1988) Blood , vol.71 , pp. 1755-1758
    • Liu, S.C.1    Zhai, S.2    Palek, J.3
  • 17
    • 0023110445 scopus 로고
    • The chemistry, pharmacology, and clinical applications of qinghaosu (artemisinin) and its derivatives
    • Luo, Z.-D., and C.-C. Shen. 1987. The chemistry, pharmacology, and clinical applications of qinghaosu (artemisinin) and its derivatives. Med. Res. Rev. 7:29-52.
    • (1987) Med. Res. Rev , vol.7 , pp. 29-52
    • Luo, Z.-D.1    Shen, C.-C.2
  • 18
    • 0028264418 scopus 로고
    • Measuring relative rates of hemoglobin oxidation and denaturation
    • Macdonald, V. W. 1994. Measuring relative rates of hemoglobin oxidation and denaturation. Methods Enzymol. 231:480-490.
    • (1994) Methods Enzymol , vol.231 , pp. 480-490
    • Macdonald, V.W.1
  • 19
    • 0037021405 scopus 로고    scopus 로고
    • Artemisinin: Mechanisms of action, resistance and toxicity
    • Meshnick, S. R. 2002. Artemisinin: mechanisms of action, resistance and toxicity. Int. J. Parasitol. 32:1655-1660.
    • (2002) Int. J. Parasitol , vol.32 , pp. 1655-1660
    • Meshnick, S.R.1
  • 20
    • 0026014249 scopus 로고
    • Artemisinin (qinghaosu): The role of intracellular hemin in its mechanism of antimalarial action
    • Meshnick, S. R., A. Thomas, A. Ranz, C.-M. Xu, and H.-Z. Pan. 1991. Artemisinin (qinghaosu): the role of intracellular hemin in its mechanism of antimalarial action. Mol. Biochem. Parasitol. 49:181-189.
    • (1991) Mol. Biochem. Parasitol , vol.49 , pp. 181-189
    • Meshnick, S.R.1    Thomas, A.2    Ranz, A.3    Xu, C.-M.4    Pan, H.-Z.5
  • 22
    • 24344443742 scopus 로고    scopus 로고
    • The therapeutic potential of semi-synthetic artemisinin and synthetic endoperoxide antimalarial agents
    • O'Neill, P. M. 2005. The therapeutic potential of semi-synthetic artemisinin and synthetic endoperoxide antimalarial agents. Exp. Opin. Investig. Drugs 14:1117-1128.
    • (2005) Exp. Opin. Investig. Drugs , vol.14 , pp. 1117-1128
    • O'Neill, P.M.1
  • 23
    • 2542640961 scopus 로고    scopus 로고
    • A medicinal chemistry perspective on artemisinin and related endoperoxides
    • O'Neill, P. M., and G. H. Posner. 2004. A medicinal chemistry perspective on artemisinin and related endoperoxides. J. Med. Chem. 47:2945-2964.
    • (2004) J. Med. Chem , vol.47 , pp. 2945-2964
    • O'Neill, P.M.1    Posner, G.H.2
  • 24
    • 0028361393 scopus 로고
    • Thermal denaturation procedures for hemoglobin
    • Olsen, K. W. 1994. Thermal denaturation procedures for hemoglobin. Methods Enzymol. 231:514-524.
    • (1994) Methods Enzymol , vol.231 , pp. 514-524
    • Olsen, K.W.1
  • 25
    • 0017164432 scopus 로고
    • The effect of ligand size and stereochemistry on the reactivity of the α and β chains within hemoglobin
    • Olson, J. S., and C. Binger. 1976. The effect of ligand size and stereochemistry on the reactivity of the α and β chains within hemoglobin. Biochim. Biophys. Acta 434:428-439.
    • (1976) Biochim. Biophys. Acta , vol.434 , pp. 428-439
    • Olson, J.S.1    Binger, C.2
  • 26
    • 33745571654 scopus 로고    scopus 로고
    • 1.25 Å resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms
    • Park, S.-Y., T. Yokoyama, N. Shibayama, Y. Shiro, and J. R. H. Tame. 2006. 1.25 Å resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms. J. Mol. Biol. 360:690-701.
    • (2006) J. Mol. Biol , vol.360 , pp. 690-701
    • Park, S.-Y.1    Yokoyama, T.2    Shibayama, N.3    Shiro, Y.4    Tame, J.R.H.5
  • 28
    • 34249323755 scopus 로고    scopus 로고
    • Artemisinin effectiveness in erythrocytes is reduced by heme and heme-containing proteins
    • Ponmee, N., T. Chuchue, P. Wilairat, Y. Yuthavong, and S. Kamchonwongpaisan. 2007. Artemisinin effectiveness in erythrocytes is reduced by heme and heme-containing proteins. Biochem. Pharmacol. 74:153-160.
    • (2007) Biochem. Pharmacol , vol.74 , pp. 153-160
    • Ponmee, N.1    Chuchue, T.2    Wilairat, P.3    Yuthavong, Y.4    Kamchonwongpaisan, S.5
  • 29
    • 23744478677 scopus 로고    scopus 로고
    • The key role of heme to trigger the antimalarial activity of trioxanes
    • Robert, A., F. Benoit-Vical, and B. Meunier. 2005. The key role of heme to trigger the antimalarial activity of trioxanes. Coord. Chem. Rev. 249:1927-1936.
    • (2005) Coord. Chem. Rev , vol.249 , pp. 1927-1936
    • Robert, A.1    Benoit-Vical, F.2    Meunier, B.3
  • 30
    • 0346725018 scopus 로고    scopus 로고
    • Alkylation of human hemoglobin A0 by the antimalarial drug artemisinin
    • Selmeczi, K., A. Robert, C. Claparols, and B. Meunier. 2004. Alkylation of human hemoglobin A0 by the antimalarial drug artemisinin. FEBS Lett. 556:245-248.
    • (2004) FEBS Lett , vol.556 , pp. 245-248
    • Selmeczi, K.1    Robert, A.2    Claparols, C.3    Meunier, B.4
  • 31
    • 15044338866 scopus 로고    scopus 로고
    • The global distribution of clinical episodes of Plasmodium falciparum malaria
    • Snow, R. W., C. A. Guerra, A. M. Noor, H. Y. Myint, and S. I. Hay. 2005. The global distribution of clinical episodes of Plasmodium falciparum malaria. Nature 434:214-217.
    • (2005) Nature , vol.434 , pp. 214-217
    • Snow, R.W.1    Guerra, C.A.2    Noor, A.M.3    Myint, H.Y.4    Hay, S.I.5
  • 32
    • 0029965273 scopus 로고    scopus 로고
    • Drug-protein interactions: Two-site binding of heterocyclic ligands to a monomeric hemoglobin
    • Stephanos, J. J. 1996. Drug-protein interactions: two-site binding of heterocyclic ligands to a monomeric hemoglobin. J. Inorg. Biochem. 62:155-169.
    • (1996) J. Inorg. Biochem , vol.62 , pp. 155-169
    • Stephanos, J.J.1
  • 35
    • 0015243223 scopus 로고
    • Studies on the reaction of isocyanides with haemproteins. I. Equilibria and kinetics of the binding to the isolated chains of human haemoglobin
    • Talbot, B., M. Brunori, E. Antonini, and J. Wyman. 1971. Studies on the reaction of isocyanides with haemproteins. I. Equilibria and kinetics of the binding to the isolated chains of human haemoglobin. J. Mol. Biol. 58:263-276.
    • (1971) J. Mol. Biol , vol.58 , pp. 263-276
    • Talbot, B.1    Brunori, M.2    Antonini, E.3    Wyman, J.4
  • 37
    • 33750309630 scopus 로고    scopus 로고
    • A new strategy for structure determination of large proteins in solution without deuteration
    • Xu, Y., Y. Zheng, J.-S. Fan, and D. Yang. 2006. A new strategy for structure determination of large proteins in solution without deuteration. Nat. Methods 3:931-937.
    • (2006) Nat. Methods , vol.3 , pp. 931-937
    • Xu, Y.1    Zheng, Y.2    Fan, J.-S.3    Yang, D.4
  • 38
    • 0027935551 scopus 로고
    • Alkylation of proteins by artemisinin. Effects of heme, pH, and drug structure
    • Yang, Y. Z., B. Little, and S. R. Meshnick. 1994. Alkylation of proteins by artemisinin. Effects of heme, pH, and drug structure. Biochem. Pharmacol. 48:569-573.
    • (1994) Biochem. Pharmacol , vol.48 , pp. 569-573
    • Yang, Y.Z.1    Little, B.2    Meshnick, S.R.3
  • 39
    • 49149110826 scopus 로고    scopus 로고
    • Heme activates artemisinin more efficiently than hemin, inorganic iron, or hemoglobin
    • Zhang, S., and G. S. Gerhard. 2008. Heme activates artemisinin more efficiently than hemin, inorganic iron, or hemoglobin. Bioorg. Med. Chem. 16:7853-7861.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 7853-7861
    • Zhang, S.1    Gerhard, G.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.