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Volumn 18, Issue 2, 2008, Pages 433-442

Binding of puerarin to human serum albumin: A spectroscopic analysis and molecular docking

Author keywords

Fluorescence quenching; Human serum albumin (HSA); Molecular docking; Puerarin

Indexed keywords

BLOOD; DICHROISM; ENERGY TRANSFER; FLUORESCENCE; QUENCHING; SPECTROSCOPIC ANALYSIS;

EID: 40549103507     PISSN: 10530509     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10895-007-0283-0     Document Type: Article
Times cited : (153)

References (41)
  • 1
    • 29344435623 scopus 로고    scopus 로고
    • Effects of puerarin on the scavenge of oxygen free radicals and the antagonism against oxidative injury
    • 1. QL Zhu AX He XR Lu 2001 Effects of puerarin on the scavenge of oxygen free radicals and the antagonism against oxidative injury Pharm J Clin PLA 17 1 4 1:CAS:528:DC%2BD3MXitlCrsbk%3D Zhu QL, He AX, Lu XR (2001) Effects of puerarin on the scavenge of oxygen free radicals and the antagonism against oxidative injury. Pharm J Clin PLA 17:1–4
    • (2001) Pharm J Clin PLA , vol.17 , pp. 1-4
    • Zhu, QL1    He, AX2    Lu, XR3
  • 2
    • 3042700415 scopus 로고    scopus 로고
    • Effects of puerarin on fatty superoxide in aged mice induced by D-galactose, Chin
    • 2. XH Xu 2003 Effects of puerarin on fatty superoxide in aged mice induced by D-galactose, Chin J Chin Mater Med 28 66 69 1:CAS:528:DC%2BD2cXksVWqurk%3D Xu XH (2003) Effects of puerarin on fatty superoxide in aged mice induced by D-galactose, Chin. J Chin Mater Med 28:66–69
    • (2003) J Chin Mater Med , vol.28 , pp. 66-69
    • Xu, XH1
  • 3
    • 3042794172 scopus 로고    scopus 로고
    • Effects of purified puerarin on voluntary alcohol intake and alcohol withdrawal symptoms in P rats receiving free access to water and alcohol
    • 3. E Benlhabib JI Baker DE Keyler AK Singh 2004 Effects of purified puerarin on voluntary alcohol intake and alcohol withdrawal symptoms in P rats receiving free access to water and alcohol J Med Food 7 180 186 15298765 10.1089/1096620041224102 1:CAS:528:DC%2BD2cXmtlSmtLo%3D Benlhabib E, Baker JI, Keyler DE, Singh AK (2004) Effects of purified puerarin on voluntary alcohol intake and alcohol withdrawal symptoms in P rats receiving free access to water and alcohol. J Med Food 7:180–186
    • (2004) J Med Food , vol.7 , pp. 180-186
    • Benlhabib, E1    Baker, JI2    Keyler, DE3    Singh, AK4
  • 4
    • 0033017247 scopus 로고    scopus 로고
    • Improvement of ocular blood flow and retinal functions with puerarin analogs
    • 4. B Xuan YH Zhou RL Yang 1999 Improvement of ocular blood flow and retinal functions with puerarin analogs J Ocular Pharmacol Ther 15 207 216 1:CAS:528:DyaK1MXjvVaqsrg%3D Xuan B, Zhou YH, Yang RL (1999) Improvement of ocular blood flow and retinal functions with puerarin analogs. J Ocular Pharmacol Ther 15:207–216
    • (1999) J Ocular Pharmacol Ther , vol.15 , pp. 207-216
    • Xuan, B1    Zhou, YH2    Yang, RL3
  • 5
    • 0038204299 scopus 로고    scopus 로고
    • Antihyperglycemic effect of puerarin in streptozotocin-induced diabetic rats
    • 5. FL Hsu IM Liu DH Kuo WC Chen HC Su JT Cheng 2003 Antihyperglycemic effect of puerarin in streptozotocin-induced diabetic rats J Nat Prod 66 788 792 12828463 10.1021/np0203887 1:CAS:528:DC%2BD3sXktVCjsL4%3D Hsu FL, Liu IM, Kuo DH, Chen WC, Su HC, Cheng JT (2003) Antihyperglycemic effect of puerarin in streptozotocin-induced diabetic rats. J Nat Prod 66:788–792
    • (2003) J Nat Prod , vol.66 , pp. 788-792
    • Hsu, FL1    Liu, IM2    Kuo, DH3    Chen, WC4    Su, HC5    Cheng, JT6
  • 6
    • 33744936020 scopus 로고    scopus 로고
    • Induction of apoptosis by puerarin in colon cancer HT-29 cells
    • 6. ZL Yu WJ Li 2006 Induction of apoptosis by puerarin in colon cancer HT-29 cells Cancer Lett 238 53 60 16055262 10.1016/j.canlet.2005.06.022 1:CAS:528:DC%2BD28XlsFOhtrk%3D Yu ZL, Li WJ (2006) Induction of apoptosis by puerarin in colon cancer HT-29 cells. Cancer Lett 238:53–60
    • (2006) Cancer Lett , vol.238 , pp. 53-60
    • Yu, ZL1    Li, WJ2
  • 7
    • 33745797747 scopus 로고    scopus 로고
    • Puerarin decreases serum total cholesterol and enhances thoracic aorta endothelial nitric oxide synthase expression in diet-induced hypercholesterolemic rats
    • 7. LP Yan SW Chan Sun-Chi Chan Albert SL Chen XJ Ma HX Xu 2006 Puerarin decreases serum total cholesterol and enhances thoracic aorta endothelial nitric oxide synthase expression in diet-induced hypercholesterolemic rats Life Sci 79 324 330 16472823 10.1016/j.lfs.2006.01.016 1:CAS:528:DC%2BD28XltlKrsLk%3D Yan LP, Chan SW, Albert Sun-Chi Chan, Chen SL, Ma XJ, Xu HX (2006) Puerarin decreases serum total cholesterol and enhances thoracic aorta endothelial nitric oxide synthase expression in diet-induced hypercholesterolemic rats. Life Sci 79:324–330
    • (2006) Life Sci , vol.79 , pp. 324-330
    • Yan, LP1    Chan, SW2    Albert, Sun-Chi Chan3    Chen, SL4    Ma, XJ5    Xu, HX6
  • 8
    • 34548177312 scopus 로고    scopus 로고
    • Transport of a cancer chemopreventive polyphenol, resveratrol: interaction with serum albumin and hemoglobin
    • 8. Z Lu Y Zhang H Liu J Yuan Z Zheng G Zou 2007 Transport of a cancer chemopreventive polyphenol, resveratrol: interaction with serum albumin and hemoglobin J Fluoresc 17 5 580 587 17597382 10.1007/s10895-007-0220-2 1:CAS:528:DC%2BD2sXpt1yktr4%3D Lu Z, Zhang Y, Liu H, Yuan J, Zheng Z, Zou G (2007) Transport of a cancer chemopreventive polyphenol, resveratrol: interaction with serum albumin and hemoglobin. J Fluoresc 17(5):580–587
    • (2007) J Fluoresc , vol.17 , Issue.5 , pp. 580-587
    • Lu, Z1    Zhang, Y2    Liu, H3    Yuan, J4    Zheng, Z5    Zou, G6
  • 9
    • 23444447825 scopus 로고    scopus 로고
    • Study of interaction between colchicines and bovine serum albumin by fluorescence quenching method
    • 9. YJ Hu Y Liu LX Zhang 2005 Study of interaction between colchicines and bovine serum albumin by fluorescence quenching method J Mol Struct 750 174 178 10.1016/j.molstruc.2005.04.032 1:CAS:528:DC%2BD2MXntVyktrs%3D Hu YJ, Liu Y, Zhang LX (2005) Study of interaction between colchicines and bovine serum albumin by fluorescence quenching method. J Mol Struct 750:174–178
    • (2005) J Mol Struct , vol.750 , pp. 174-178
    • Hu, YJ1    Liu, Y2    Zhang, LX3
  • 10
    • 11844253806 scopus 로고    scopus 로고
    • Flavonoid-serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy
    • 10. C Dufour O Dangles 2005 Flavonoid-serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy Biochim Biophys Acta 1721 164 173 15652191 1:CAS:528:DC%2BD2MXivVSrtw%3D%3D Dufour C, Dangles O (2005) Flavonoid-serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy. Biochim Biophys Acta 1721:164–173
    • (2005) Biochim Biophys Acta , vol.1721 , pp. 164-173
    • Dufour, C1    Dangles, O2
  • 11
    • 33745280263 scopus 로고    scopus 로고
    • Characterization of the interaction between human serum albumin and morin
    • 11. MX Xie M Long Y Liu C Qin YD Wang 2006 Characterization of the interaction between human serum albumin and morin Biochim Biophys Acta 1760 1184 1191 16750302 1:CAS:528:DC%2BD28Xmt1Orsrc%3D Xie MX, Long M, Liu Y, Qin C, Wang YD (2006) Characterization of the interaction between human serum albumin and morin. Biochim Biophys Acta 1760:1184–1191
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 1184-1191
    • Xie, MX1    Long, M2    Liu, Y3    Qin, C4    Wang, YD5
  • 12
    • 33644936244 scopus 로고    scopus 로고
    • A spectroscopic study of the interaction of isoflavones with human serum albumin
    • 12. HG Mahesha SA Sighn N Srinivasan RAG Appu 2006 A spectroscopic study of the interaction of isoflavones with human serum albumin FEBS J 273 451 467 16420470 10.1111/j.1742-4658.2005.05071.x 1:CAS:528:DC%2BD28Xis1Giurk%3D Mahesha HG, Sighn SA, Srinivasan N, Appu RAG (2006) A spectroscopic study of the interaction of isoflavones with human serum albumin. FEBS J 273:451–467
    • (2006) FEBS J , vol.273 , pp. 451-467
    • Mahesha, HG1    Sighn, SA2    Srinivasan, N3    Appu, RAG4
  • 13
    • 0035933789 scopus 로고    scopus 로고
    • Crystal structure analysis of warfarin binding to human serum albumin—anatomy of drug site I
    • 13. I Petitpas AA Bhattacharya S Twine M East S Curry 2001 Crystal structure analysis of warfarin binding to human serum albumin—anatomy of drug site I J Biol Chem 276 22804 22809 11285262 10.1074/jbc.M100575200 1:CAS:528:DC%2BD3MXkvVamt7c%3D 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, I1    Bhattacharya, AA2    Twine, S3    East, M4    Curry, S5
  • 14
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • 14. XM He DC Carter 1992 Atomic structure and chemistry of human serum albumin Nature 358 209 215 1630489 10.1038/358209a0 1:CAS:528:DyaK38XlsVGmurg%3D He XM, Carter DC (1992) Atomic structure and chemistry of human serum albumin. Nature 358:209–215
    • (1992) Nature , vol.358 , pp. 209-215
    • He, XM1    Carter, DC2
  • 15
    • 0033842504 scopus 로고    scopus 로고
    • Five recombinant fragments of human serum albumin—tools for the characterization of the warfarin binding site
    • 15. M Dockal M Chang DC Carter F Rüker 2000 Five recombinant fragments of human serum albumin—tools for the characterization of the warfarin binding site Protein Sci 9 1455 1465 10975567 1:CAS:528:DC%2BD3cXmt1Oms70%3D 10.1110/ps.9.8.1455 Dockal M, Chang M, Carter Rüker DCF (2000) Five recombinant fragments of human serum albumin—tools for the characterization of the warfarin binding site. Protein Sci 9:1455–1465
    • (2000) Protein Sci , vol.9 , pp. 1455-1465
    • Dockal, M1    Chang, M2    Carter, DC3    Rüker, F4
  • 16
    • 0027209990 scopus 로고
    • Volatile anesthetics compete for common binding sites on bovine serum albumin: a 19F-NMR study
    • 16. BW Dubois SF Cherian AS Evers 1993 Volatile anesthetics compete for common binding sites on bovine serum albumin: a 19 F-NMR study Proc Natl Acad Sci USA 90 6478 6482 8341659 10.1073/pnas.90.14.6478 1:CAS:528:DyaK3sXltVygtb8%3D Dubois BW, Cherian SF, Evers AS (1993) Volatile anesthetics compete for common binding sites on bovine serum albumin: a 19 F-NMR study. Proc Natl Acad Sci USA 90:6478–6482
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6478-6482
    • Dubois, BW1    Cherian, SF2    Evers, AS3
  • 17
    • 33750625101 scopus 로고    scopus 로고
    • Pharmacokinetic profile of the isoflavone puerarin after acute and repeated administration of a novel kudzu extract to human volunteers
    • 17. DM Penetar CJ Teter Z Ma M Tracy DY Lee SE Lukas 2006 Pharmacokinetic profile of the isoflavone puerarin after acute and repeated administration of a novel kudzu extract to human volunteers J Altern Complement Med 12 543 548 16884345 10.1089/acm.2006.12.543 Penetar DM, Teter CJ, Ma Z, Tracy M, Lee DY, Lukas SE (2006) Pharmacokinetic profile of the isoflavone puerarin after acute and repeated administration of a novel kudzu extract to human volunteers. J Altern Complement Med 12:543–548
    • (2006) J Altern Complement Med , vol.12 , pp. 543-548
    • Penetar, DM1    Teter, CJ2    Ma, Z3    Tracy, M4    Lee, DY5    Lukas, SE6
  • 18
    • 23944480016 scopus 로고    scopus 로고
    • Interaction of daunomycin antibiotic with human serum albumin: investigation by resonant mirror biosensor technique, fluorescence spectroscopy and molecular modeling methods
    • 18. K Tang YM Qin AH Lin X Hu GL Zou 2005 Interaction of daunomycin antibiotic with human serum albumin: investigation by resonant mirror biosensor technique, fluorescence spectroscopy and molecular modeling methods J Pharm Biomed Anal 39 404 410 15964731 10.1016/j.jpba.2005.03.045 1:CAS:528:DC%2BD2MXpsVCntrs%3D Tang K, Qin YM, Lin AH, Hu X, Zou GL (2005) Interaction of daunomycin antibiotic with human serum albumin: investigation by resonant mirror biosensor technique, fluorescence spectroscopy and molecular modeling methods. J Pharm Biomed Anal 39:404–410
    • (2005) J Pharm Biomed Anal , vol.39 , pp. 404-410
    • Tang, K1    Qin, YM2    Lin, AH3    Hu, X4    Zou, GL5
  • 19
    • 85121084012 scopus 로고    scopus 로고
    • 19. Yuan JL, Lv Z, Liu ZG, Hu Z, Zou GL (2007) Study on interaction between apigenin and human serum albumin by spectroscopy and molecular modeling. J Photochem Photobiol A Chem (in press)
  • 20
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • 20. GM Morris DS Goodsell RS Halliday R Huey WE Hart AJ Belew RK Olson 1998 Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function J Comput Chem 19 1639 1662 10.1002/(SICI)1096-987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B 1:CAS:528:DyaK1cXntFemur4%3D Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, Belew RK Olson AJ (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem 19:1639–1662
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, GM1    Goodsell, DS2    Halliday, RS3    Huey, R4    Hart, WE5    Belew RK Olson, AJ6
  • 21
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • 21. HM Berman J Westbrook Z Feng G Gilliland TN Bhat H Weissig IN Shindyalov PE Bourne 2000 The Protein Data Bank Nucleic Acids Res 28 235 242 10592235 10.1093/nar/28.1.235 1:CAS:528:DC%2BD3cXhvVKjt7w%3D Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE (2000) The Protein Data Bank. Nucleic Acids Res 28:235–242
    • (2000) Nucleic Acids Res , vol.28 , pp. 235-242
    • Berman, HM1    Westbrook, J2    Feng, Z3    Gilliland, G4    Bhat, TN5    Weissig, H6    Shindyalov, IN7    Bourne, PE8
  • 23
    • 0032867556 scopus 로고    scopus 로고
    • Partially folded state of the disulfide-reduced form of human serum albumin as an intermediate for reversible denaturation
    • 23. JY Lee M Hirose 1999 Partially folded state of the disulfide-reduced form of human serum albumin as an intermediate for reversible denaturation J Biol Chem 274 29303 29310 10.1074/jbc.274.41.29303 Lee JY, Hirose M (1999) Partially folded state of the disulfide-reduced form of human serum albumin as an intermediate for reversible denaturation. J Biol Chem 274:29303–29310
    • (1999) J Biol Chem , vol.274 , pp. 29303-29310
    • Lee, JY1    Hirose, M2
  • 24
    • 0042929255 scopus 로고    scopus 로고
    • The principle of bioinorganic chemistry
    • 24. P Yang F Gao 2002 The principle of bioinorganic chemistry Science Beijing Yang P, Gao F (2002) The principle of bioinorganic chemistry. Science, Beijing
    • (2002)
    • Yang, P1    Gao, F2
  • 25
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • 25. YH Chen JT Yang HM Martinez 1972 Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion Biochemistry 11 4120 4131 4343790 10.1021/bi00772a015 1:CAS:528:DyaE3sXht12ltw%3D%3D Chen YH, Yang JT, Martinez HM (1972) Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11:4120–4131
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, YH1    Yang, JT2    Martinez, HM3
  • 26
    • 0034730631 scopus 로고    scopus 로고
    • Inhaled anesthetic binding sites in human serum albumin
    • 26. RG Eckenhoff E Charles 2000 Inhaled anesthetic binding sites in human serum albumin J Biol Chem 275 30439–30444 10896670 10.1074/jbc.M005052200 Eckenhoff RG, Charles E (2000) Inhaled anesthetic binding sites in human serum albumin. J Biol Chem 275:30439–30444
    • (2000) J Biol Chem , vol.275 , pp. 30439–30444
    • Eckenhoff, RG1    Charles, E2
  • 27
    • 34547093163 scopus 로고    scopus 로고
    • Characterization of the myricetin-human serum albumin complex by spectroscopic and molecular modeling approaches
    • 27. C Qin M-X Xie Y Liu 2007 Characterization of the myricetin-human serum albumin complex by spectroscopic and molecular modeling approaches Biomacromolecules 8 2182 2189 17559264 10.1021/bm070319c 1:CAS:528:DC%2BD2sXmtlGgs7Y%3D Qin C, Xie M-X, Liu Y (2007) Characterization of the myricetin-human serum albumin complex by spectroscopic and molecular modeling approaches. Biomacromolecules 8:2182–2189
    • (2007) Biomacromolecules , vol.8 , pp. 2182-2189
    • Qin, C1    Xie, M-X2    Liu, Y3
  • 28
    • 0005885530 scopus 로고
    • Recent advances in molecular luminescence analysis
    • 28. JN Miller 1979 Recent advances in molecular luminescence analysis Proc Anal Div Chem Soc 16 203 208 1:CAS:528:DyaE1MXmt1ajsr4%3D Miller JN (1979) Recent advances in molecular luminescence analysis. Proc Anal Div Chem Soc 16:203–208
    • (1979) Proc Anal Div Chem Soc , vol.16 , pp. 203-208
    • Miller, JN1
  • 29
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • 29. RE Maurice AG Camillo 1981 Fluorescence quenching studies with proteins Anal Biochem 114 199 212 10.1016/0003-2697(81)90474-7 Maurice RE, Camillo AG (1981) Fluorescence quenching studies with proteins. Anal Biochem 114:199–212
    • (1981) Anal Biochem , vol.114 , pp. 199-212
    • Maurice, RE1    Camillo, AG2
  • 30
    • 5044238048 scopus 로고    scopus 로고
    • Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method
    • 30. JN Tian JQ Liu WY He ZD Hu XJ Yao XG Cheng 2004 Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method Biomacromolecules 5 1956 1961 15360311 10.1021/bm049668m 1:CAS:528:DC%2BD2cXmslSns70%3D Tian JN, Liu JQ, He WY, Hu ZD, Yao XJ, Cheng XG (2004) Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method. Biomacromolecules 5:1956–1961
    • (2004) Biomacromolecules , vol.5 , pp. 1956-1961
    • Tian, JN1    Liu, JQ2    He, WY3    Hu, ZD4    Yao, XJ5    Cheng, XG6
  • 31
    • 0004106021 scopus 로고
    • The methods of fluorescence analysis
    • 31. GZ Chen XZ Huang 1990 The methods of fluorescence analysis 2 Science Beijing Chen GZ, Huang XZ (1990) The methods of fluorescence analysis, 2nd edn. Science, Beijing
    • (1990)
    • Chen, GZ1    Huang, XZ2
  • 32
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: force contributing to stability
    • 32. PD Ross S Subramanian 1981 Thermodynamics of protein association reactions: force contributing to stability Biochemistry 20 3096 3102 7248271 10.1021/bi00514a017 1:CAS:528:DyaL3MXktF2qsb0%3D Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions: force contributing to stability. Biochemistry 20:3096–3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, PD1    Subramanian, S2
  • 33
    • 85121074858 scopus 로고    scopus 로고
    • 33. Viviane M, Yves E, Johan H, Yvan M, Antoine V (1981) Fluorimetric analysis of binding of warfarin to human serum albumin
  • 34
    • 34548821894 scopus 로고    scopus 로고
    • The spectrophysics of warfarin: implications for protein binding
    • 34. CG Karlsson AM Rosengren PO Andersson IA Nicholls 2007 The spectrophysics of warfarin: implications for protein binding J Phys Chem B 111 10520 10528 17691835 10.1021/jp072505i 1:CAS:528:DC%2BD2sXovFWgur4%3D Karlsson CG, Rosengren AM, Andersson PO, Nicholls IA (2007) The spectrophysics of warfarin: implications for protein binding. J Phys Chem B 111:10520–10528
    • (2007) J Phys Chem B , vol.111 , pp. 10520-10528
    • Karlsson, CG1    Rosengren, AM2    Andersson, PO3    Nicholls, IA4
  • 35
    • 0017661379 scopus 로고
    • Conjugated polyene fatty acids as fluorescent probes: binding to bovine serum albumin
    • 35. LA Sklar BS Hudson RD Simoni 1977 Conjugated polyene fatty acids as fluorescent probes: binding to bovine serum albumin Biochemistry 16 5100 5108 911814 10.1021/bi00642a024 1:CAS:528:DyaE1cXhvFKr Sklar LA, Hudson BS, Simoni RD (1977) Conjugated polyene fatty acids as fluorescent probes: binding to bovine serum albumin. Biochemistry 16:5100–5108
    • (1977) Biochemistry , vol.16 , pp. 5100-5108
    • Sklar, LA1    Hudson, BS2    Simoni, RD3
  • 36
    • 0037123057 scopus 로고    scopus 로고
    • Interaction of ochratoxin A with human serum albumin: preferential binding of the dianion and pH effects
    • 36. YV Ilichev JL Perry JD Simon 2002 Interaction of ochratoxin A with human serum albumin: preferential binding of the dianion and pH effects J Phys Chem (B) 106 452 459 1:CAS:528:DC%2BD3MXptV2mtr0%3D Ilichev YV, Perry JL, Simon JD (2002) Interaction of ochratoxin A with human serum albumin: preferential binding of the dianion and pH effects. J Phys Chem (B) 106:452–459
    • (2002) J Phys Chem (B) , vol.106 , pp. 452-459
    • Ilichev, YV1    Perry, JL2    Simon, JD3
  • 37
    • 0003636421 scopus 로고    scopus 로고
    • New trends in fluorescence spectroscopy
    • 37. B Valeur JC Brochon 1999 New trends in fluorescence spectroscopy 6 Springer Berlin Valeur B, Brochon JC (1999) New trends in fluorescence spectroscopy, 6th edn. Springer, Berlin
    • (1999)
    • Valeur, B1    Brochon, JC2
  • 38
    • 0037300833 scopus 로고    scopus 로고
    • Probing the binding of the flavonoid, quercetin to human serum albumin by circular dichroism, electronic absorption spectroscopy and molecular modelling methods
    • 38. F Zsila Z Bikadi M Simonyi 2003 Probing the binding of the flavonoid, quercetin to human serum albumin by circular dichroism, electronic absorption spectroscopy and molecular modelling methods Biochem Pharmacol 65 447 456 12527338 10.1016/S0006-2952(02)01521-6 1:CAS:528:DC%2BD3sXivVKhsw%3D%3D Zsila F, Bikadi Z, Simonyi M (2003) Probing the binding of the flavonoid, quercetin to human serum albumin by circular dichroism, electronic absorption spectroscopy and molecular modelling methods. Biochem Pharmacol 65:447–456
    • (2003) Biochem Pharmacol , vol.65 , pp. 447-456
    • Zsila, F1    Bikadi, Z2    Simonyi, M3
  • 39
    • 33845216262 scopus 로고    scopus 로고
    • Acid-base equilibrium of puerarin in CTAB micelles
    • 39. JQ Xi R Guo 2007 Acid-base equilibrium of puerarin in CTAB micelles J Pharm Biomed Anal 43 111 118 16935449 10.1016/j.jpba.2006.06.028 1:CAS:528:DC%2BD28Xht12rt7fE Xi JQ, Guo R (2007) Acid-base equilibrium of puerarin in CTAB micelles. J Pharm Biomed Anal 43:111–118
    • (2007) J Pharm Biomed Anal , vol.43 , pp. 111-118
    • Xi, JQ1    Guo, R2
  • 40
    • 0034602966 scopus 로고    scopus 로고
    • Conformational transitions of the three recombinant domains of human serum albumin depending on pH
    • 40. D Michael DC Carter F Rüker 2000 Conformational transitions of the three recombinant domains of human serum albumin depending on pH J Biol Chem 275 3042 3050 10.1074/jbc.275.5.3042 Michael D, Carter DC, Rüker F (2000) Conformational transitions of the three recombinant domains of human serum albumin depending on pH. J Biol Chem 275:3042–3050
    • (2000) J Biol Chem , vol.275 , pp. 3042-3050
    • Michael, D1    Carter, DC2    Rüker, F3
  • 41
    • 25144505772 scopus 로고    scopus 로고
    • Structural basis of the drug-binding specificity of human serum albumin
    • 41. G Jamie ZA Patricia P Isabelle AA Bhattacharya O Masaki C Stephen 2005 Structural basis of the drug-binding specificity of human serum albumin J Mol Biol 353 38 52 10.1016/j.jmb.2005.07.075 1:CAS:528:DC%2BD2MXhtVensrbJ Jamie G, Patricia ZA, Isabelle P, Bhattacharya AA, Masaki O, Stephen C (2005) Structural basis of the drug-binding specificity of human serum albumin. J Mol Biol 353:38–52
    • (2005) J Mol Biol , vol.353 , pp. 38-52
    • Jamie, G1    Patricia, ZA2    Isabelle, P3    Bhattacharya, AA4    Masaki, O5    Stephen, C6


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