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Volumn 23, Issue 2, 2013, Pages 333-338

Investigation of binding properties of umbelliferone (7hydroxycoumarin) to lysozyme

Author keywords

Fluorescence quenching; FRET; Lysozyme; Umbelliferone

Indexed keywords

FLUORESCENCE QUENCHING; FRET; HYDROPHOBIC INTERACTIONS; RESONANCE ENERGY TRANSFER; STERN-VOLMER EQUATION; THERMODYNAMIC PARAMETER; UMBELLIFERONE; UMBELLIFERONE (7-HYDROXYCOUMARIN);

EID: 84879696055     PISSN: 10530509     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10895-012-1151-0     Document Type: Article
Times cited : (7)

References (26)
  • 1
    • 0033116136 scopus 로고    scopus 로고
    • Studies of fuorescent dyes: Part 1. An investigation of the electronic spectral properties of substituted coumarins
    • 10.1016/S0143-7208(99)00012-1 1:CAS:528:DyaK1MXivFKhs70%3D
    • Christie RM, Liu C-H (1999) Studies of fuorescent dyes: Part 1. An investigation of the electronic spectral properties of substituted coumarins. Dyes Pigments 42:85-93
    • (1999) Dyes Pigments , vol.42 , pp. 85-93
    • Christie, R.M.1    Liu, C.-H.2
  • 2
    • 0034299555 scopus 로고    scopus 로고
    • I -benzimidazolyl) coumarins
    • 10.1016/S0143-7208(00)00066-8 1:CAS:528:DC%2BD3cXotlWku7c%3D
    • I -benzimidazolyl) coumarins. Dyes Pigments 47:79-89
    • (2000) Dyes Pigments , vol.47 , pp. 79-89
    • Christie, R.M.1    Liu, C.-H.2
  • 3
    • 0008264289 scopus 로고    scopus 로고
    • Spectroscopy and photophysics of 4-and 7-hydroxycoumarins and their thione analogs
    • 10.1016/S0022-2860(01)00458-6
    • Seixas de Melo J, Fernandes PF (2001) Spectroscopy and photophysics of 4-and 7-hydroxycoumarins and their thione analogs. J Mol Struct 565-566:69-78
    • (2001) J Mol Struct , vol.565-566 , pp. 69-78
    • Seixas De Melo, J.1    Fernandes, P.F.2
  • 4
    • 26444433849 scopus 로고    scopus 로고
    • Theoretical investigations of the UV spectra of coumarin derivatives
    • 10.1016/j.cplett.2005.08.135 1:CAS:528:DC%2BD2MXhtVOks77O
    • Preat J, Jacquemin D, Perpete EA (2005) Theoretical investigations of the UV spectra of coumarin derivatives. Chem Phys Lett 415:20-24
    • (2005) Chem Phys Lett , vol.415 , pp. 20-24
    • Preat, J.1    Jacquemin, D.2    Perpete, E.A.3
  • 5
    • 51649083455 scopus 로고    scopus 로고
    • Interaction of thyroxine with 7 hydroxycoumarin: A fluorescence quenching study
    • 18523878 10.1007/s10895-008-0382-6
    • Gök E, Öztürk C, Akbay N (2008) Interaction of thyroxine with 7 hydroxycoumarin: A fluorescence quenching study. J Fluoresc 18:781-785
    • (2008) J Fluoresc , vol.18 , pp. 781-785
    • Gök, E.1    Öztürk, C.2    Akbay, N.3
  • 6
    • 60749114975 scopus 로고    scopus 로고
    • Effect of umbelliferone (7-hydroxycoumarin, 7-HOC) on the enzymatic, edematogenic and necrotic activities of secretory phospholipase A2(sPLA2) isolated from Crotalus durissus collilineatus venom
    • 19470355 10.1016/j.toxicon.2008.12.018 1:CAS:528:DC%2BD1MXisVGit7k%3D
    • Toyama DO, Marangoni S, Diz-Filho EBS, Oliveira SCB, Toyama MH (2009) Effect of umbelliferone (7-hydroxycoumarin, 7-HOC) on the enzymatic, edematogenic and necrotic activities of secretory phospholipase A2(sPLA2) isolated from Crotalus durissus collilineatus venom. Toxicon 53:417-426
    • (2009) Toxicon , vol.53 , pp. 417-426
    • Toyama, D.O.1    Marangoni, S.2    Diz-Filho, E.B.S.3    Oliveira, S.C.B.4    Toyama, M.H.5
  • 8
    • 62849117688 scopus 로고    scopus 로고
    • Probing the binding of 8-Acetyl-7-hydroxycoumarin to human serum albumin by spectroscopic methods and molecular modeling
    • 10.1016/j.saa.2009.01.023
    • Li D, Ji B, Sun H (2009) Probing the binding of 8-Acetyl-7- hydroxycoumarin to human serum albumin by spectroscopic methods and molecular modeling. Spectrochim Acta Part A 73:35-40
    • (2009) Spectrochim Acta Part A , vol.73 , pp. 35-40
    • Li, D.1    Ji, B.2    Sun, H.3
  • 9
    • 79952489321 scopus 로고    scopus 로고
    • Spectroscopic studies of 7, 8-dihydroxy-4-methylcoumarin and its interaction with bovin serum albumin
    • 10.1016/j.jlumin.2010.12.021 1:CAS:528:DC%2BC3MXjtVCqtL4%3D
    • Hussein BHM (2011) Spectroscopic studies of 7, 8-dihydroxy-4- methylcoumarin and its interaction with bovin serum albumin. J Lumin 131:900-908
    • (2011) J Lumin , vol.131 , pp. 900-908
    • Hussein, B.H.M.1
  • 10
    • 77953236810 scopus 로고    scopus 로고
    • Interaction of alpinetin with bovine serum albumin: Probing of the mechanism and binding site by spectroscopic methods
    • 10.1016/j.saa.2010.04.009
    • Zhang G, Zhao N, Hu X, Tian J (2010) Interaction of alpinetin with bovine serum albumin: Probing of the mechanism and binding site by spectroscopic methods. Spectrochim Acta Part A 76:410-417
    • (2010) Spectrochim Acta Part A , vol.76 , pp. 410-417
    • Zhang, G.1    Zhao, N.2    Hu, X.3    Tian, J.4
  • 11
    • 70449084682 scopus 로고    scopus 로고
    • Interaction of kaempferol with human serum albumin: A fluorescence and circular dichroism study
    • 19853398 10.1016/j.jpba.2009.09.037 1:CAS:528:DC%2BD1MXhtl2jtr3N
    • Matei I, Hillebrand M (2010) Interaction of kaempferol with human serum albumin: A fluorescence and circular dichroism study. J Pharm Biomed Anal 51:768-773
    • (2010) J Pharm Biomed Anal , vol.51 , pp. 768-773
    • Matei, I.1    Hillebrand, M.2
  • 12
    • 33746563581 scopus 로고    scopus 로고
    • Studies of the interaction between palmatine hydrochloride and human serum albumin by fluorescence quenching method
    • 16549318 10.1016/j.jpba.2006.01.028 1:CAS:528:DC%2BD28Xks1equ70%3D
    • Wang Y-Q, Zhang H-M, Zhang GC (2006) Studies of the interaction between palmatine hydrochloride and human serum albumin by fluorescence quenching method. J Pharm Biomed Anal 41:1041-1046
    • (2006) J Pharm Biomed Anal , vol.41 , pp. 1041-1046
    • Wang, Y.-Q.1    Zhang, H.-M.2    Zhang, G.C.3
  • 13
    • 70349307040 scopus 로고    scopus 로고
    • Study on the binding behavior of lysozyme with cephalosporin analogues by fluorescence spectroscopy
    • 19343485 10.1007/s10895-009-0477-8 1:CAS:528:DC%2BD1MXhtFGnsrbM
    • Wang Z, Tan X, Chen D, Yue Q, Song Z (2009) Study on the binding behavior of lysozyme with cephalosporin analogues by fluorescence spectroscopy. J Fluoresc 19:801-808
    • (2009) J Fluoresc , vol.19 , pp. 801-808
    • Wang, Z.1    Tan, X.2    Chen, D.3    Yue, Q.4    Song, Z.5
  • 14
    • 38149063469 scopus 로고    scopus 로고
    • Study on the interaction mechanism of lysozyme and bromophenol blue by fluorescence spectroscopy
    • 17682927 10.1007/s10895-007-0228-7 1:CAS:528:DC%2BD1cXjtlyis7Y%3D
    • Yue Q, Niu L, Li X, Shao X, Xie X, Song Z (2008) Study on the interaction mechanism of lysozyme and bromophenol blue by fluorescence spectroscopy. J Fluoresc 18:11-15
    • (2008) J Fluoresc , vol.18 , pp. 11-15
    • Yue, Q.1    Niu, L.2    Li, X.3    Shao, X.4    Xie, X.5    Song, Z.6
  • 15
    • 76349097336 scopus 로고    scopus 로고
    • Investigation of the interactions of lysozyme and trypsin with biphenol A using spectroscopic methods
    • 10.1016/j.saa.2009.12.071
    • Wang Y-Q, Chen T-T, Zhang H-M (2010) Investigation of the interactions of lysozyme and trypsin with biphenol A using spectroscopic methods. Spectrochim Acta Part A 75:1130-1137
    • (2010) Spectrochim Acta Part A , vol.75 , pp. 1130-1137
    • Wang, Y.-Q.1    Chen, T.-T.2    Zhang, H.-M.3
  • 16
    • 79551568051 scopus 로고    scopus 로고
    • Study on the interaction between cinnamic acid and lysozyme
    • 10.1016/j.molstruc.2010.11.053 1:CAS:528:DC%2BC3MXhtlKqtb4%3D
    • Zhang H-M, Chen J, Zhou Q-H, Shi Y-Q, Wang Y-Q (2011) Study on the interaction between cinnamic acid and lysozyme. J Mol Struct 987:7-12
    • (2011) J Mol Struct , vol.987 , pp. 7-12
    • Zhang, H.-M.1    Chen, J.2    Zhou, Q.-H.3    Shi, Y.-Q.4    Wang, Y.-Q.5
  • 17
    • 79960189580 scopus 로고    scopus 로고
    • Effect of pH on the interaction of baicalein with lysozyme by spectroscopic approaches
    • 10.1016/j.jphotobiol.2011.04.009 1:CAS:528:DC%2BC3MXoslWrt7s%3D
    • Li D, Zhang T, Xu C, Ji B (2011) Effect of pH on the interaction of baicalein with lysozyme by spectroscopic approaches. J Photochem Photobiol B Biol 104:414-424
    • (2011) J Photochem Photobiol B Biol , vol.104 , pp. 414-424
    • Li, D.1    Zhang, T.2    Xu, C.3    Ji, B.4
  • 18
    • 84155164993 scopus 로고    scopus 로고
    • Investigation on the pH-dependent binding of vitamin B12 and lysozyme by fluorescence and absorbance
    • 10.1016/j.molstruc.2011.10.028 1:CAS:528:DC%2BC3MXhs1CgtL%2FN
    • Li D, Yang Y, Cao X, Xu C, Ji B (2012) Investigation on the pH-dependent binding of vitamin B12 and lysozyme by fluorescence and absorbance. J Mol Struct 1007:102-112
    • (2012) J Mol Struct , vol.1007 , pp. 102-112
    • Li, D.1    Yang, Y.2    Cao, X.3    Xu, C.4    Ji, B.5
  • 19
    • 84055178630 scopus 로고    scopus 로고
    • Investigation on the interactions of silymarin to bovine serum albumin and lysozyme by fluorescence and absorbance
    • 10.1016/j.jlumin.2011.11.021 1:CAS:528:DC%2BC38Xnt1alsw%3D%3D
    • Pang B, Bi S, Wang Y, Yan L, Wang T (2012) Investigation on the interactions of silymarin to bovine serum albumin and lysozyme by fluorescence and absorbance. J Lumin 132:895-900
    • (2012) J Lumin , vol.132 , pp. 895-900
    • Pang, B.1    Bi, S.2    Wang, Y.3    Yan, L.4    Wang, T.5
  • 20
    • 72049092673 scopus 로고    scopus 로고
    • Interaction of anthraquinone dyes with lysozyme: Evidences from spectroscopic and docking studies
    • 19939563 10.1016/j.jhazmat.2009.10.107 1:CAS:528:DC%2BD1MXhsFOqsLjE
    • Paramaguru G, Kathiravan A, Selvaraj S, Venuvanalingam P, Renganathan R (2010) Interaction of anthraquinone dyes with lysozyme: Evidences from spectroscopic and docking studies. J Hazard Mater 175:985-991
    • (2010) J Hazard Mater , vol.175 , pp. 985-991
    • Paramaguru, G.1    Kathiravan, A.2    Selvaraj, S.3    Venuvanalingam, P.4    Renganathan, R.5
  • 21
    • 70349312672 scopus 로고    scopus 로고
    • A study of the interaction between malachite green and lysozyme by steady-state fluorescence
    • 10.1007/s10895-009-0475-x
    • Ding F, Liu W, Liu F, Li Z-Y, Sun Y (2009) A study of the interaction between malachite green and lysozyme by steady-state fluorescence. J Fluoresc 19:1783-791
    • (2009) J Fluoresc , vol.19 , pp. 1783-1791
    • Ding, F.1    Liu, W.2    Liu, F.3    Li, Z.-Y.4    Sun, Y.5
  • 24
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • 7248271 10.1021/bi00514a017 1:CAS:528:DyaL3MXktF2qsb0%3D
    • Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry 20:3096-3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 25
    • 56949096774 scopus 로고    scopus 로고
    • The fluorescence resonance energy transfer between dye compound in micellar media
    • 10.1016/j.dyepig.2008.10.002
    • AydIn BM, Acar M, ArIk M, Onganer Y (2009) The fluorescence resonance energy transfer between dye compound in micellar media. Dyes Pigments 81:156-160
    • (2009) Dyes Pigments , vol.81 , pp. 156-160
    • Aydin, B.M.1    Acar, M.2    Arik, M.3    Onganer, Y.4
  • 26
    • 71749096547 scopus 로고    scopus 로고
    • Fluorescence resonance energy-transfer affects the determination of the affinity between ligand and proteins obtained by fluorescence quenching method
    • 10.1016/j.saa.2009.09.003
    • Xiao J, Wei X, Wang Y, Liu C (2009) Fluorescence resonance energy-transfer affects the determination of the affinity between ligand and proteins obtained by fluorescence quenching method. Spectrochim Acta Part A 74:977-982
    • (2009) Spectrochim Acta Part A , vol.74 , pp. 977-982
    • Xiao, J.1    Wei, X.2    Wang, Y.3    Liu, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.