메뉴 건너뛰기




Volumn 21, Issue 5, 2011, Pages 1879-1886

Binding of quercetin to lysozyme as probed by spectroscopic analysis and molecular simulation

Author keywords

Fluorescence quenching; Lysozyme; Molecular simulation; Quercetin

Indexed keywords

ACCESSIBLE SURFACE AREAS; ACTIVE SITE; BINDING CONSTANT; BINDING PROCESS; ENTHALPY CHANGE; ENTROPY CHANGES; FLUORESCENCE QUENCHING; FLUORESCENCE RESONANCE ENERGY TRANSFER; HYDROGEN INTERACTION; HYDROPHOBIC INTERACTIONS; LYSOZYME; MOLECULAR SIMULATIONS; QUERCETIN; STATIC QUENCHING; SYNCHRONOUS FLUORESCENCE SPECTROSCOPY; THERMODYNAMIC PARAMETER; TRYPTOPHAN RESIDUES; UV-VIS ABSORPTION SPECTROSCOPY;

EID: 80052964795     PISSN: 10530509     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10895-011-0884-5     Document Type: Article
Times cited : (22)

References (35)
  • 2
    • 0001868668 scopus 로고
    • Vitamin P: Flavonols as vitamins
    • 10.1038/138027a0 1:CAS:528:DyaA28XkvVaitw%3D%3D
    • ST Rusznyak A Szent-Gyorgyi 1936 Vitamin P: flavonols as vitamins Nature 138 27 27 10.1038/138027a0 1:CAS:528:DyaA28XkvVaitw%3D%3D
    • (1936) Nature , vol.138 , pp. 27-27
    • Rusznyak, S.T.1    Szent-Gyorgyi, A.2
  • 3
    • 0035415723 scopus 로고    scopus 로고
    • Anti-inflammatory properties of plant flavonoids. Effects of rutin, quercetin and hesperidin on adjuvant arthritis in rat
    • DOI 10.1016/S0014-827X(01)01111-9, PII S0014827X01011119
    • T Guardia AE Rotelli AO Juarez LE Pelzer 2001 Anti-inflammatory properties of plant flavonoids. Effects of rutin, quercetin and hesperidin on adjuvant arthritis in rat Farmaco 56 683 687 11680812 10.1016/S0014-827X(01) 01111-9 1:CAS:528:DC%2BD3MXnsVSksbc%3D (Pubitemid 32916351)
    • (2001) Farmaco , vol.56 , Issue.9 , pp. 683-687
    • Guardia, T.1    Rotelli, A.E.2    Juarez, A.O.3    Pelzer, L.E.4
  • 4
    • 0029610477 scopus 로고
    • Review of the biology of quercetin and related bioflavonoids
    • DOI 10.1016/0278-6915(95)00077-1
    • JV Formica W Regelson 1995 Review of the biology of quercetin and related bioflavonoids Food Chem Toxicol 33 1061 1080 8847003 10.1016/0278-6915(95) 00077-1 1:CAS:528:DyaK28Xht1Cgsw%3D%3D (Pubitemid 26009773)
    • (1995) Food and Chemical Toxicology , vol.33 , Issue.12 , pp. 1061-1080
    • Formica, J.V.1
  • 7
    • 33748413614 scopus 로고    scopus 로고
    • Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence
    • DOI 10.1002/mnfr.200600013
    • HM Rawel SK Frey K Meidtner J Kroll FJ Schweigert 2006 Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence Mol Nutr Food Res 50 705 713 16835869 10.1002/mnfr.200600013 1:CAS:528:DC%2BD28XovFKrur8%3D (Pubitemid 44342467)
    • (2006) Molecular Nutrition and Food Research , vol.50 , Issue.8 , pp. 705-713
    • Rawel, H.M.1    Frey, S.K.2    Meidtner, K.3    Kroll, J.4    Schweigert, F.J.5
  • 8
    • 20844443677 scopus 로고    scopus 로고
    • Binding of selected phenolic compounds to proteins
    • DOI 10.1021/jf0480290
    • HM Rawel K Meidtner J Kroll 2005 Binding of selected phenolic compounds to proteins J Agr Food Chem 53 4228 4235 10.1021/jf0480290 1:CAS:528: DC%2BD2MXjtFGhsLw%3D (Pubitemid 40936789)
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.10 , pp. 4228-4235
    • Rawel, H.M.1    Meidtner, K.2    Kroll, J.3
  • 9
    • 1542315306 scopus 로고    scopus 로고
    • Conformational changes of lysozyme refolding intermediates and implications for aggregation and renaturation
    • DOI 10.1016/j.biocel.2003.08.015, PII S1357272503003091
    • Z Gu X Zhu S Ni Z Su HM Zhou 2004 Conformational changes of lysozyme refolding intermediates and implications for aggregation and renaturation Int J Biochem Cell Biol 36 795 805 15006632 10.1016/j.biocel.2003.08.015 1:CAS:528:DC%2BD2cXhvFSmtLg%3D (Pubitemid 38299395)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.5 , pp. 795-805
    • Gu, Z.1    Zhu, X.2    Ni, S.3    Su, Z.4    Zhou, H.-M.5
  • 10
    • 33644540629 scopus 로고    scopus 로고
    • Unfolding of lysozyme induced by urea and guanidine hydrochloride studied by "phase diagram" method of fluorescence
    • F Yang L Liang 2003 Unfolding of lysozyme induced by urea and guanidine hydrochloride studied by "phase diagram" method of fluorescence Acta Chim Sinica 61 803 807 1:CAS:528:DC%2BD3sXkvVant7c%3D (Pubitemid 44662764)
    • (2003) Acta Chimica Sinica , vol.61 , Issue.6 , pp. 803-807
    • Yang, F.1    Liang, Y.2    Yang Jr., F.3
  • 11
    • 70349252283 scopus 로고    scopus 로고
    • Simultaneous determination of glucose and choline based on the intrinsic fluorescence of the enzymes
    • 19089602 10.1007/s10895-008-0448-5 1:CAS:528:DC%2BD1MXosVGisLk%3D
    • I Sanz-Vicente JJ Romero S de Marcos M Ostra C Ubide J Galbán 2009 Simultaneous determination of glucose and choline based on the intrinsic fluorescence of the enzymes J Fluoresc 19 583 591 19089602 10.1007/s10895-008- 0448-5 1:CAS:528:DC%2BD1MXosVGisLk%3D
    • (2009) J Fluoresc , vol.19 , pp. 583-591
    • Sanz-Vicente, I.1    Romero, J.J.2    De Marcos, S.3    Ostra, M.4    Ubide, C.5    Galbán, J.6
  • 12
    • 0033992505 scopus 로고    scopus 로고
    • Iron and citrate interactions with hen egg white lysozyme
    • DOI 10.1016/S0308-8146(99)00147-8, PII S0308814699001478
    • T Croguennec F Nau D Molle Y Le Graet G Brule 2000 Iron and citrate interactions with hen egg white lysozyme Food Chem 68 29 35 10.1016/S0308- 8146(99)00147-8 1:CAS:528:DyaK1MXns12kur8%3D (Pubitemid 29488674)
    • (2000) Food Chemistry , vol.68 , Issue.1 , pp. 29-35
    • Croguennec, T.1    Nau, F.2    Molle, D.3    Le Graet, Y.4    Brule, G.5
  • 14
    • 33845997673 scopus 로고    scopus 로고
    • version 0.99, USA, San Carlos
    • Delano WL (2004) PyMOL software, version 0.99, USA, San Carlos
    • (2004) PyMOL Software
    • Delano, W.L.1
  • 16
    • 35548983013 scopus 로고    scopus 로고
    • Studies on the binding of nevadensin to human serum albumin by molecular spectroscopy and modeling
    • DOI 10.1016/j.molstruc.2007.01.020, PII S0022286007000622
    • DJ Li JF Zhu J Jin XJ Yao 2007 Studies on the binding of nevadensin to human serum albumin by molecular spectroscopy and simulation J Mol Struct 846 34 41 10.1016/j.molstruc.2007.01.020 1:CAS:528:DC%2BD2sXht1OrurrF (Pubitemid 350016013)
    • (2007) Journal of Molecular Structure , vol.846 , Issue.1-3 , pp. 34-41
    • Li, D.1    Zhu, J.2    Jin, J.3    Yao, X.4
  • 18
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules
    • 4795686 10.1021/bi00745a020 1:CAS:528:DyaE3sXlsVeks78%3D
    • JR Lakowicz G Weber 1973 Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules Biochemistry 12 4161 4170 4795686 10.1021/bi00745a020 1:CAS:528:DyaE3sXlsVeks78%3D
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.R.1    Weber, G.2
  • 19
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process
    • 10.1021/j100809a020 1:CAS:528:DyaF38XktVygtLw%3D
    • WR Ware 1962 Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process J Phys Chem 66 455 458 10.1021/j100809a020 1:CAS:528:DyaF38XktVygtLw%3D
    • (1962) J Phys Chem , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 20
    • 3242709482 scopus 로고    scopus 로고
    • Investigation of the interaction between flavonoids and human serum albumin
    • DOI 10.1016/j.molstruc.2004.05.026, PII S0022286004004223
    • SY Bi L Ding Y Tian DQ Song X Zhou X Liu, et al. 2004 Investigation of the interaction between flavonoids and human serum albumin J Mol Struct 703 37 45 10.1016/j.molstruc.2004.05.026 1:CAS:528:DC%2BD2cXmtVSrsLw%3D (Pubitemid 38953410)
    • (2004) Journal of Molecular Structure , vol.703 , Issue.1-3 , pp. 37-45
    • Bi, S.1    Ding, L.2    Tian, Y.3    Song, D.4    Zhou, X.5    Liu, X.6    Zhang, H.7
  • 21
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • 7248271 10.1021/bi00514a017 1:CAS:528:DyaL3MXktF2qsb0%3D
    • PD Ross S Subramanian 1981 Thermodynamics of protein association reactions: forces contributing to stability Biochemistry 20 3096 3102 7248271 10.1021/bi00514a017 1:CAS:528:DyaL3MXktF2qsb0%3D
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 22
    • 19444375863 scopus 로고    scopus 로고
    • Interaction of wogonin with bovine serum albumin
    • DOI 10.1016/j.bmc.2005.02.065, PII S0968089605002397
    • J Tian J Liu Z Hu X Chen 2005 Interaction of wogonin with bovine serum albumin Bioorg Med Chem 13 4124 4129 15911327 10.1016/j.bmc.2005.02.065 1:CAS:528:DC%2BD2MXks1Gjs70%3D (Pubitemid 40725046)
    • (2005) Bioorganic and Medicinal Chemistry , vol.13 , Issue.12 , pp. 4124-4129
    • Tian, J.1    Liu, J.2    Hu, Z.3    Chen, X.4
  • 23
    • 0027491794 scopus 로고
    • Study of interaction of carprofen and its enantiomers with human serum albumin. - I. Mechanism of binding studied by dialysis and spectroscopic methods
    • DOI 10.1016/0006-2952(93)90576-I
    • MH Rahman T Maruyama T Okada K Yamasaki M Otagiri 1993 Study of interaction of carprofen and its enantiomers with human serum albumin-I: mechanism of binding studied by dialysis and spectroscopic methods Biochem Pharmacol 46 1721 1731 7504487 10.1016/0006-2952(93)90576-I 1:CAS:528: DyaK2cXht1CisLc%3D (Pubitemid 23349019)
    • (1993) Biochemical Pharmacology , vol.46 , Issue.10 , pp. 1721-1731
    • Rahman, M.H.1    Maruyama, T.2    Okada, T.3    Yamasaki, K.4    Otagiri, M.5
  • 24
    • 0014118693 scopus 로고
    • Energy transfer: A spectroscopic ruler
    • 5233469 10.1073/pnas.58.2.719 1:CAS:528:DyaF1cXoslGlsQ%3D%3D
    • L Stryer RP Haugland 1967 Energy transfer: a spectroscopic ruler Proc Natl Acad Sci USA 58 719 726 5233469 10.1073/pnas.58.2.719 1:CAS:528: DyaF1cXoslGlsQ%3D%3D
    • (1967) Proc Natl Acad Sci USA , vol.58 , pp. 719-726
    • Stryer, L.1    Haugland, R.P.2
  • 27
    • 0014593973 scopus 로고
    • Intramolecular singlet excitation transfer. Applications to polypeptides
    • 5346376 10.1021/bi00838a005 1:CAS:528:DyaF1MXltFKlsb8%3D
    • J Eisinger B Feuer AA Lamola 1969 Intramolecular singlet excitation transfer. Applications to polypeptides Biochemistry 8 3908 3915 5346376 10.1021/bi00838a005 1:CAS:528:DyaF1MXltFKlsb8%3D
    • (1969) Biochemistry , vol.8 , pp. 3908-3915
    • Eisinger, J.1    Feuer, B.2    Lamola, A.A.3
  • 28
    • 0015163780 scopus 로고
    • Long-range nonradiative transfer of electronic excitation energy in proteins and polypeptides
    • 4331120 10.1146/annurev.bi.40.070171.000503 1:CAS:528:DyaE3MXlt1KisL8%3D
    • IZ Steinberg 1971 Long-range nonradiative transfer of electronic excitation energy in proteins and polypeptides Annu Rev Biochem 40 83 114 4331120 10.1146/annurev.bi.40.070171.000503 1:CAS:528:DyaE3MXlt1KisL8%3D
    • (1971) Annu Rev Biochem , vol.40 , pp. 83-114
    • Steinberg, I.Z.1
  • 29
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • 4583619 10.1111/j.1751-1097.1973.tb06422.x 1:STN:280: DyaE2c%2FhsVCrtQ%3D%3D
    • EA Burstein NS Vedenkina MN Ivkova 1973 Fluorescence and the location of tryptophan residues in protein molecules Photochem Photobiol 18 263 279 4583619 10.1111/j.1751-1097.1973.tb06422.x 1:STN:280:DyaE2c%2FhsVCrtQ%3D%3D
    • (1973) Photochem Photobiol , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 30
    • 0036148318 scopus 로고    scopus 로고
    • Fluorescence studies on PAMAM dendrimers interactions with bovine serum albumin
    • DOI 10.1016/S1567-5394(01)00170-0, PII S1567539401001700
    • B Klajnert M Bryszewska 2002 Fluorescence studies on PAMAM dendrimers interactions with bovine serum albumin Bioelectrochemistry 55 33 35 11786335 10.1016/S1567-5394(01)00170-0 1:CAS:528:DC%2BD38Xls1eguw%3D%3D (Pubitemid 34084746)
    • (2002) Bioelectrochemistry , vol.55 , Issue.1-2 , pp. 33-35
    • Klajnert, B.1    Bryszewska, M.2
  • 31
    • 27644475219 scopus 로고    scopus 로고
    • Interaction of cromolyn sodium with human serum albumin: A fluorescence quenching study
    • DOI 10.1016/j.bmc.2005.07.039, PII S0968089605006681
    • YJ Hu Y Liu ZB Pi SS Qu 2005 Interaction of cromolyn sodium with human serum albumin: a fluorescence quenching study Bioorg Med Chem 13 6609 6614 16126393 10.1016/j.bmc.2005.07.039 1:CAS:528:DC%2BD2MXhtFyksrnF (Pubitemid 41571205)
    • (2005) Bioorganic and Medicinal Chemistry , vol.13 , Issue.24 , pp. 6609-6614
    • Hu, Y.-J.1    Liu, Y.2    Pi, Z.-B.3    Qu, S.-S.4
  • 33
    • 0013801241 scopus 로고
    • The position of the active tryptophan residue in lysozyme
    • 5861328 1:CAS:528:DyaF28XivVyhtA%3D%3D
    • K Hayashi T Imoto G Funatsu M Funatsu 1965 The position of the active tryptophan residue in lysozyme J Biochem 58 227 235 5861328 1:CAS:528: DyaF28XivVyhtA%3D%3D
    • (1965) J Biochem , vol.58 , pp. 227-235
    • Hayashi, K.1    Imoto, T.2    Funatsu, G.3    Funatsu, M.4
  • 34
    • 0016696047 scopus 로고
    • Tryptophan fluorescence lifetimes in lysozyme
    • C Rmoso LS Förster 1975 Tryptophan fluorescence lifetimes in lysozyme J Biol Chem 250 3738 3745
    • (1975) J Biol Chem , vol.250 , pp. 3738-3745
    • Rmoso, C.1    Förster, L.S.2
  • 35
    • 13444292204 scopus 로고    scopus 로고
    • Effect of Chinese medicine alpinetin on the structure of human serum albumin
    • DOI 10.1016/j.bmc.2004.11.038
    • WY He Y Li CX Xue ZD Hu XG Chen FL Sheng 2005 Effect of Chinese medicine alpinetin on the structure of human serum albumin Bioorg Med Chem 13 1837 1845 15698801 10.1016/j.bmc.2004.11.038 1:CAS:528:DC%2BD2MXhtVKjsL4%3D (Pubitemid 40215271)
    • (2005) Bioorganic and Medicinal Chemistry , vol.13 , Issue.5 , pp. 1837-1845
    • He, W.1    Li, Y.2    Xue, C.3    Hu, Z.4    Chen, X.5    Sheng, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.