메뉴 건너뛰기




Volumn 278, Issue 4, 2011, Pages 654-662

Ibuprofen binding to secondary sites allosterically modulates the spectroscopic and catalytic properties of human serum heme-albumin

Author keywords

allostery; human serum heme albumin; ibuprofen binding; modulation of reactivity and spectroscopic properties; recombinant truncated human serum heme albumin (Asp1 Glu382)

Indexed keywords

ASPARTIC ACID; FATTY ACID; FATTY ACID 2; FATTY ACID 3; FATTY ACID 4; FATTY ACID 6; GLUTAMINE; HEME; HUMAN SERUM ALBUMIN; IBUPROFEN; PEROXYNITRITE; RECOMBINANT PROTEIN; TRUNCATED HUMAN SERUM ALBUMIN; UNCLASSIFIED DRUG;

EID: 79751502747     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07986.x     Document Type: Article
Times cited : (40)

References (40)
  • 1
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • Sudlow G, Birkett DJ, &, Wade DN, (1975) The characterization of two specific drug binding sites on human serum albumin. Mol Pharmacol 11, 824-832.
    • (1975) Mol Pharmacol , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 3
    • 0037591928 scopus 로고    scopus 로고
    • Beyond expansion: Structural studies on the transport roles of human serum albumin
    • Curry S, (2002) Beyond expansion: structural studies on the transport roles of human serum albumin. Vox Sang 83 (Suppl), 1.
    • (2002) Vox Sang , vol.83 , Issue.SUPPL. , pp. 1
    • Curry, S.1
  • 4
    • 0036599564 scopus 로고    scopus 로고
    • Practical aspects of the ligand-binding and enzymatic properties of human serum albumin
    • DOI 10.1248/bpb.25.695
    • Kragh-Hansen U, Chuang VT, &, Otagiri M, (2002) Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biol Pharm Bull 25, 695-704. (Pubitemid 40036701)
    • (2002) Biological and Pharmaceutical Bulletin , vol.25 , Issue.6 , pp. 695-704
    • Krach-Hansen, U.1    Chuang, V.T.G.2    Otagiri, M.3
  • 8
    • 77951977240 scopus 로고    scopus 로고
    • Allostery in a monomeric protein: The case of human serum heme-albumin
    • Ascenzi P, &, Fasano M, (2010) Allostery in a monomeric protein: the case of human serum heme-albumin. Biophys Chem 148, 16-22.
    • (2010) Biophys Chem , vol.148 , pp. 16-22
    • Ascenzi, P.1    Fasano, M.2
  • 9
    • 70350455500 scopus 로고    scopus 로고
    • Lessons from the crystallographic analysis of small molecule binding to human serum albumin
    • Curry S, (2009) Lessons from the crystallographic analysis of small molecule binding to human serum albumin. Drug Metab Pharmacokinet 24, 342-357.
    • (2009) Drug Metab Pharmacokinet , vol.24 , pp. 342-357
    • Curry, S.1
  • 10
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • DOI 10.1038/1869
    • Curry S, Mandelkov H, Brick P, &, Franks N, (1998) Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat Struct Biol 5, 827-835. (Pubitemid 28402087)
    • (1998) Nature Structural Biology , vol.5 , Issue.9 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4
  • 11
    • 0034624021 scopus 로고    scopus 로고
    • Binding of the general anesthetics propofol and halothane to human serum albumin: High resolution crystal structures
    • DOI 10.1074/jbc.M005460200
    • Bhattacharya AA, Curry S, &, Franks NP, (2000) Binding of the general anesthetics propofol and halothane to human serum albumin: high resolution crystal structures. J Biol Chem 275, 38731-38738. (Pubitemid 32009208)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.49 , pp. 38731-38738
    • Bhattacharya, A.A.1    Curry, S.2    Franks, N.P.3
  • 12
    • 0034634370 scopus 로고    scopus 로고
    • Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin
    • Bhattacharya AA, Grüne T, &, Curry S, (2000) Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. J Mol Biol 303, 721-732.
    • (2000) J Mol Biol , vol.303 , pp. 721-732
    • Bhattacharya, A.A.1    Grüne, T.2    Curry, S.3
  • 13
    • 0033842504 scopus 로고    scopus 로고
    • Five recombinant fragments of human serum albumin - Tools for the characterization of the warfarin binding site
    • Dockal M, Chang M, Carter DC, &, Rüker F, (2000) Five recombinant fragments of human serum albumin: tools for the characterization of the warfarin binding site. Protein Sci 9, 1455-1465. (Pubitemid 30659184)
    • (2000) Protein Science , vol.9 , Issue.8 , pp. 1455-1465
    • Dockal, M.1    Chang, M.2    Carter, D.C.3    Ruker, F.4
  • 14
    • 0035933789 scopus 로고    scopus 로고
    • Crystal structure analysis of warfarin binding to human serum albumin: Anatomy of drug site i
    • Petitpas I, Bhattacharya AA, Twine S, East M, &, Curry S, (2001) Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I. J Biol Chem 276, 22804-22809.
    • (2001) J Biol Chem , vol.276 , pp. 22804-22809
    • Petitpas, I.1    Bhattacharya, A.A.2    Twine, S.3    East, M.4    Curry, S.5
  • 15
    • 0036804804 scopus 로고    scopus 로고
    • How do fatty acids cause allosteric binding of drugs to human serum albumin?
    • DOI 10.1023/A:1020496314081
    • Chuang VTG, &, Otagiri M, (2002) How do fatty acids cause allosteric binding of drugs to human serum albumin? Pharm Res 19, 1458-1464. (Pubitemid 35266549)
    • (2002) Pharmaceutical Research , vol.19 , Issue.10 , pp. 1458-1464
    • Chuang, V.T.G.1    Otagiri, M.2
  • 16
    • 1542345719 scopus 로고    scopus 로고
    • Fatty acid interactions with proteins: What X-ray crystal and NMR solution structures tell us
    • DOI 10.1016/j.plipres.2003.09.002, PII S0163782703000523
    • Hamilton JA, (2004) Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us. Prog Lipid Res 43, 177-199. (Pubitemid 38299192)
    • (2004) Progress in Lipid Research , vol.43 , Issue.3 , pp. 177-199
    • Hamilton, J.A.1
  • 17
    • 33746253976 scopus 로고    scopus 로고
    • Location of high and low affinity fatty acid binding sites on human serum albumin revealed by NMR drug-competition analysis
    • DOI 10.1016/j.jmb.2006.06.028, PII S0022283606007509
    • Simard JR, Zunszain PA, Hamilton JA, &, Curry S, (2006) Location of high and low affinity fatty acid binding sites on human serum albumin revealed by NMR drug-competition analysis. J Mol Biol 361, 336-351. (Pubitemid 44092787)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.2 , pp. 336-351
    • Simard, J.R.1    Zunszain, P.A.2    Hamilton, J.A.3    Curry, S.4
  • 18
    • 51349131362 scopus 로고    scopus 로고
    • Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation
    • Nicoletti FP, Howes BD, Fittipaldi M, Fanali G, Fasano M, Ascenzi P, &, Smulevich G, (2008) Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation. J Am Chem Soc 130, 11677-11688.
    • (2008) J Am Chem Soc , vol.130 , pp. 11677-11688
    • Nicoletti, F.P.1    Howes, B.D.2    Fittipaldi, M.3    Fanali, G.4    Fasano, M.5    Ascenzi, P.6    Smulevich, G.7
  • 19
    • 63049107798 scopus 로고    scopus 로고
    • Allosteric and binding properties of Asp1-Glu382 truncated recombinant human serum albumin: An optical and NMR spectroscopic investigation
    • Fanali G, Pariani G, Ascenzi P, &, Fasano M, (2009) Allosteric and binding properties of Asp1-Glu382 truncated recombinant human serum albumin: an optical and NMR spectroscopic investigation. EJB J 276, 2241-2250.
    • (2009) EJB J , vol.276 , pp. 2241-2250
    • Fanali, G.1    Pariani, G.2    Ascenzi, P.3    Fasano, M.4
  • 20
    • 67651039712 scopus 로고    scopus 로고
    • Ibuprofen modulates allosterically NO dissociation from ferrous nitrosylated human serum heme-albumin by binding to three sites
    • Ascenzi P, di Masi A, de Sanctis G, Coletta M, &, Fasano M, (2009) Ibuprofen modulates allosterically NO dissociation from ferrous nitrosylated human serum heme-albumin by binding to three sites. Biochem Biophys Res Commun 387, 83-86.
    • (2009) Biochem Biophys Res Commun , vol.387 , pp. 83-86
    • Ascenzi, P.1    Di Masi, A.2    De Sanctis, G.3    Coletta, M.4    Fasano, M.5
  • 22
    • 40849114506 scopus 로고    scopus 로고
    • Abacavir and warfarin modulate allosterically kinetics of NO dissociation from ferrous nitrosylated human serum heme-albumin
    • Ascenzi P, Imperi F, Coletta M, &, Fasano M, (2008) Abacavir and warfarin modulate allosterically kinetics of NO dissociation from ferrous nitrosylated human serum heme-albumin. Biochem Biophys Res Commun 369, 686-691.
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 686-691
    • Ascenzi, P.1    Imperi, F.2    Coletta, M.3    Fasano, M.4
  • 23
    • 0035210356 scopus 로고    scopus 로고
    • Effect of ibuprofen and warfarin on the allosteric properties of haem-human serum albumin: A spectrospic study
    • DOI 10.1046/j.0014-2956.2001.02569.x
    • Baroni S, Mattu M, Vannini A, Cipollone R, Aime S, Ascenzi P, &, Fasano M, (2001) Effect of ibuprofen and warfarin on the allosteric properties of haem-human serum albumin: a spectroscopic study. Eur J Biochem 268, 6214-6220. (Pubitemid 33132042)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.23 , pp. 6214-6220
    • Baroni, S.1    Mattu, M.2    Vannini, A.3    Cipollone, R.4    Aime, S.5    Ascenzi, P.6    Fasano, M.7
  • 24
    • 0031006612 scopus 로고    scopus 로고
    • Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase
    • DOI 10.1021/bi970201o
    • Kharitonov VG, Sharma VS, Magde D, &, Koesling D, (1997) Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase. Biochemistry 36, 6814-6818. (Pubitemid 27242342)
    • (1997) Biochemistry , vol.36 , Issue.22 , pp. 6814-6818
    • Kharitonov, V.G.1    Sharma, V.S.2    Magde, D.3    Koesling, D.4
  • 25
    • 25444527458 scopus 로고    scopus 로고
    • Allosteric modulation of myristate and Mn(III)heme binding to human serum albumin: Optical and NMR spectroscopy characterization
    • DOI 10.1111/j.1742-4658.2005.04883.x
    • Fanali G, Fesce R, Agrati C, Ascenzi P, &, Fasano M, (2005) Allosteric modulation of myristate and Mn(III)heme binding to human serum albumin: optical and NMR spectroscopy characterization. EJB J 272, 4672-4683. (Pubitemid 41366990)
    • (2005) FEBS Journal , vol.272 , Issue.18 , pp. 4672-4683
    • Fanali, G.1    Fesce, R.2    Agrati, C.3    Ascenzi, P.4    Fasano, M.5
  • 26
    • 34548138940 scopus 로고    scopus 로고
    • Modulation of heme and myristate binding to human serum albumin by anti-HIV drugs: An optical and NMR spectroscopic study
    • DOI 10.1111/j.1742-4658.2007.05978.x
    • Fanali G, Bocedi A, Ascenzi P, &, Fasano M, (2007) Modulation of heme and myristate binding to human serum albumin by anti-HIV drugs. An optical and NMR spectroscopic study. EJB J 274, 4491-4502. (Pubitemid 47301710)
    • (2007) FEBS Journal , vol.274 , Issue.17 , pp. 4491-4502
    • Fanali, G.1    Bocedi, A.2    Ascenzi, P.3    Fasano, M.4
  • 27
    • 34347219413 scopus 로고    scopus 로고
    • 1H-NMR relaxometric study
    • DOI 10.1016/j.bpc.2007.05.002, PII S030146220700110X
    • Fanali G, Ascenzi P, &, Fasano M, (2007) Effect of prototypic drugs ibuprofen and warfarin on global chaotropic unfolding of human serum heme-albumin: a fast-field-cycling 1H-NMR relaxometric study. Biophys Chem 129, 29-35. (Pubitemid 47002119)
    • (2007) Biophysical Chemistry , vol.129 , Issue.1 , pp. 29-35
    • Fanali, G.1    Ascenzi, P.2    Fasano, M.3
  • 29
    • 0029688736 scopus 로고    scopus 로고
    • Syntheses of pure tetramethylammonium peroxynitrite
    • Bohle DS, Glassbrenner PA, &, Hansert B, (1996) Syntheses of pure tetramethylammonium peroxynitrite. Methods Enzymol 269, 302-311.
    • (1996) Methods Enzymol , vol.269 , pp. 302-311
    • Bohle, D.S.1    Glassbrenner, P.A.2    Hansert, B.3
  • 30
    • 0029834589 scopus 로고    scopus 로고
    • Syntheses of peroxynitrite: To go with the flow or on solid grounds?
    • Koppenol WH, Kissner R, &, Beckman JS, (1996) Syntheses of peroxynitrite: to go with the flow or on solid grounds? Methods Enzymol 269, 296-302. (Pubitemid 26295717)
    • (1996) Methods in Enzymology , vol.269 , pp. 296-302
    • Koppenol, W.H.1    Kissner, R.2    Beckman, J.S.3
  • 31
    • 0037348406 scopus 로고    scopus 로고
    • The mechanism of the peroxynitrite-mediated oxidation of myoglobin in the absence and presence of carbon dioxide
    • DOI 10.1021/tx025595l
    • Herold S, Exner M, &, Boccini F, (2003) The mechanism of the peroxynitrite mediated oxidation of myoglobin in the absence and presence of carbon dioxide. Chem Res Toxicol 16, 390-402. (Pubitemid 36373704)
    • (2003) Chemical Research in Toxicology , vol.16 , Issue.3 , pp. 390-402
    • Herold, S.1    Exner, M.2    Boccini, F.3
  • 32
    • 3042771981 scopus 로고    scopus 로고
    • Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants
    • DOI 10.1021/ja0493300
    • Herold S, Kalinga S, Matsui T, &, Watanabe Y, (2004) Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants. J Am Chem Soc 126, 6945-6955. (Pubitemid 38855393)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.22 , pp. 6945-6955
    • Herold, S.1    Kalinga, S.2    Matsui, T.3    Watanabe, Y.4
  • 33
    • 33845750255 scopus 로고    scopus 로고
    • Abacavir modulates peroxynitrite-mediated oxidation of ferrous nitrosylated human serum heme-albumin
    • DOI 10.1016/j.bbrc.2006.12.041, PII S0006291X06026994
    • Ascenzi P, &, Fasano M, (2007) Abacavir modulates peroxynitrite-mediated oxidation of ferrous nitrosylated human serum heme-albumin. Biochem Biophys Res Commun 353, 469-474. (Pubitemid 46014587)
    • (2007) Biochemical and Biophysical Research Communications , vol.353 , Issue.2 , pp. 469-474
    • Ascenzi, P.1    Fasano, M.2
  • 34
    • 35148877224 scopus 로고    scopus 로고
    • Scavenging of reactive nitrogen species by mycobacterial truncated hemoglobins
    • Ascenzi P, &, Visca P, (2008) Scavenging of reactive nitrogen species by mycobacterial truncated hemoglobins. Methods Enzymol 436, 317-337.
    • (2008) Methods Enzymol , vol.436 , pp. 317-337
    • Ascenzi, P.1    Visca, P.2
  • 35
    • 42949134909 scopus 로고    scopus 로고
    • The chemistry of peroxynitrite: Implications for biological activity
    • Goldstein S, &, Merényi G, (2008) The chemistry of peroxynitrite: implications for biological activity. Methods Enzymol 436, 49-61.
    • (2008) Methods Enzymol , vol.436 , pp. 49-61
    • Goldstein, S.1    Merényi, G.2
  • 37
    • 21944443058 scopus 로고    scopus 로고
    • Chemistry of peroxynitrites and peroxynitrates
    • Goldstein S, Lind J, &, Merényi G, (2005) Chemistry of peroxynitrites and peroxynitrates. Chem Rev 105, 2457-2470.
    • (2005) Chem Rev , vol.105 , pp. 2457-2470
    • Goldstein, S.1    Lind, J.2    Merényi, G.3
  • 38
    • 0034794453 scopus 로고    scopus 로고
    • Peroxynitrite isomerization catalyzed by His64 myoglobin mutants
    • DOI 10.1021/ja010111d
    • Herold S, Matsui T, &, Watanabe Y, (2001) Peroxynitrite isomerization catalyzed by His64 myoglobin mutants. J Am Chem Soc 123, 4085-4086. (Pubitemid 32899496)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.17 , pp. 4085-4086
    • Herold, S.1    Matsui, T.2    Watanabe, Y.3
  • 39
    • 0344844492 scopus 로고    scopus 로고
    • Metmyoglobin and methemoglobin catalyze the isomerization of peroxynitrite to nitrate
    • DOI 10.1021/bi0350349
    • Herold S, &, Kalinga S, (2003) Metmyoglobin and methemoglobin catalyze the isomerization of peroxynitrite to nitrate. Biochemistry 42, 14036-14046. (Pubitemid 37466629)
    • (2003) Biochemistry , vol.42 , Issue.47 , pp. 14036-14046
    • Herold, S.1    Shivashankar, K.2
  • 40
    • 3042673067 scopus 로고    scopus 로고
    • Crystal structural analysis of human serum albumin complexed with hemin and fatty acid
    • Zunszain PA, Ghuman J, Komatsu T, Tsuchida E, &, Curry S, (2003) Crystal structural analysis of human serum albumin complexed with hemin and fatty acid. BMC Struct Biol 3, 6.
    • (2003) BMC Struct Biol , vol.3 , pp. 6
    • Zunszain, P.A.1    Ghuman, J.2    Komatsu, T.3    Tsuchida, E.4    Curry, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.