메뉴 건너뛰기




Volumn 162, Issue , 2016, Pages 14-23

Characterizing the binding interaction between antimalarial artemether (AMT) and bovine serum albumin (BSA): Spectroscopic and molecular docking methods

Author keywords

Artemether; Bovine serum albumin; Interaction; Molecular docking; Spectroscopy

Indexed keywords

ARTEMETHER; BOVINE SERUM ALBUMIN; ANTIMALARIAL AGENT; ARTEMISININ DERIVATIVE; PROTEIN BINDING;

EID: 84975810797     PISSN: 10111344     EISSN: 18732682     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2016.06.025     Document Type: Article
Times cited : (119)

References (32)
  • 1
    • 84930617005 scopus 로고    scopus 로고
    • Spectroscopic study on the interaction of resveratrol and pterostilbene with human serum albumin
    • [1] Nair, M.S., Spectroscopic study on the interaction of resveratrol and pterostilbene with human serum albumin. J. Photochem. Photobiol. B 149 (2015), 58–67.
    • (2015) J. Photochem. Photobiol. B , vol.149 , pp. 58-67
    • Nair, M.S.1
  • 3
    • 84874055632 scopus 로고    scopus 로고
    • Spectral characterization of the binding and conformational changes of bovine serum albumin upon interaction with an anti-fungal drug, methylparaben
    • [3] Naik, K.M., Nandibewoor, S.T., Spectral characterization of the binding and conformational changes of bovine serum albumin upon interaction with an anti-fungal drug, methylparaben. Spectrochim. Acta A 105 (2013), 418–423.
    • (2013) Spectrochim. Acta A , vol.105 , pp. 418-423
    • Naik, K.M.1    Nandibewoor, S.T.2
  • 4
    • 84929326649 scopus 로고    scopus 로고
    • Binding interaction of sorafenib with bovine serum albumin: Spectroscopic methodologies and molecular docking
    • [4] Shi, J.-H., Chen, J., Wang, J., Zhu, Y.-Y., Wang, Q., Binding interaction of sorafenib with bovine serum albumin: Spectroscopic methodologies and molecular docking. Spectrochim. Acta A 149 (2015), 630–637.
    • (2015) Spectrochim. Acta A , vol.149 , pp. 630-637
    • Shi, J.-H.1    Chen, J.2    Wang, J.3    Zhu, Y.-Y.4    Wang, Q.5
  • 7
    • 11244303574 scopus 로고    scopus 로고
    • Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study
    • [7] Papadopoulou, A., Green, R.J., Frazier, R.A., Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study. J. Agric. Food Chem. 53 (2005), 158–163.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 158-163
    • Papadopoulou, A.1    Green, R.J.2    Frazier, R.A.3
  • 8
    • 84907546294 scopus 로고    scopus 로고
    • Interaction of norfloxacin with bovine serum albumin studied by different spectrometric methods; displacement studies, molecular modeling and chemometrics approaches
    • [8] Naseri, A., Hosseini, S., Rasoulzadeh, F., Rashidi, M.-R., Zakery, M., Khayamian, T., Interaction of norfloxacin with bovine serum albumin studied by different spectrometric methods; displacement studies, molecular modeling and chemometrics approaches. J. Lumin. 157 (2015), 104–112.
    • (2015) J. Lumin. , vol.157 , pp. 104-112
    • Naseri, A.1    Hosseini, S.2    Rasoulzadeh, F.3    Rashidi, M.-R.4    Zakery, M.5    Khayamian, T.6
  • 9
    • 84862544008 scopus 로고    scopus 로고
    • Synthesis, crystal structures of novel complexes of rare earth with norfloxacin, interaction with DNA and BSA
    • [9] Li, S., Wang, Y., Lin, Q., Liu, W., Ding, J., Wang, Y., Synthesis, crystal structures of novel complexes of rare earth with norfloxacin, interaction with DNA and BSA. J. Rare Earths 30 (2012), 460–466.
    • (2012) J. Rare Earths , vol.30 , pp. 460-466
    • Li, S.1    Wang, Y.2    Lin, Q.3    Liu, W.4    Ding, J.5    Wang, Y.6
  • 10
    • 77949490963 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction and sonodynamic damage of neutral red (NR) to bovine serum albumin (BSA)
    • [10] Liu, B., Guo, Y., Wang, J., Xu, R., Wang, X., Wang, D., Zhang, L., Xu, Y., Spectroscopic studies on the interaction and sonodynamic damage of neutral red (NR) to bovine serum albumin (BSA). J. Lumin. 130 (2010), 1036–1043.
    • (2010) J. Lumin. , vol.130 , pp. 1036-1043
    • Liu, B.1    Guo, Y.2    Wang, J.3    Xu, R.4    Wang, X.5    Wang, D.6    Zhang, L.7    Xu, Y.8
  • 11
    • 0037041475 scopus 로고    scopus 로고
    • Linear sweep voltammetric determination of protein based on its interaction with Alizarin Red S
    • [11] Sun, W., Jiao, K., Linear sweep voltammetric determination of protein based on its interaction with Alizarin Red S. Talanta 56 (2002), 1073–1080.
    • (2002) Talanta , vol.56 , pp. 1073-1080
    • Sun, W.1    Jiao, K.2
  • 13
    • 84856579594 scopus 로고    scopus 로고
    • Binding interaction between plasma protein bovine serum albumin and flexible charge transfer fluorophore: a spectroscopic study in combination with molecular docking and molecular dynamics simulation
    • [13] Jana, S., Dalapati, S., Ghosh, S., Guchhait, N., Binding interaction between plasma protein bovine serum albumin and flexible charge transfer fluorophore: a spectroscopic study in combination with molecular docking and molecular dynamics simulation. J. Photochem. Photobiol. A 231 (2012), 19–27.
    • (2012) J. Photochem. Photobiol. A , vol.231 , pp. 19-27
    • Jana, S.1    Dalapati, S.2    Ghosh, S.3    Guchhait, N.4
  • 14
    • 84872466478 scopus 로고    scopus 로고
    • Intermolecular interaction of prednisolone with bovine serum albumin: spectroscopic and molecular docking methods
    • [14] Shi, J.H., Zhu, Y.Y., Wang, J., Chen, J., Shen, Y.J., Intermolecular interaction of prednisolone with bovine serum albumin: spectroscopic and molecular docking methods. Spectrochim. Acta A 103 (2013), 287–294.
    • (2013) Spectrochim. Acta A , vol.103 , pp. 287-294
    • Shi, J.H.1    Zhu, Y.Y.2    Wang, J.3    Chen, J.4    Shen, Y.J.5
  • 15
    • 84884259548 scopus 로고    scopus 로고
    • Characterization of interaction between isoliquiritigenin and bovine serum albumin: spectroscopic and molecular docking methods
    • [15] Shi, J.H., Wang, J., Zhu, Y.Y., Chen, J., Characterization of interaction between isoliquiritigenin and bovine serum albumin: spectroscopic and molecular docking methods. J. Lumin. 145 (2014), 643–650.
    • (2014) J. Lumin. , vol.145 , pp. 643-650
    • Shi, J.H.1    Wang, J.2    Zhu, Y.Y.3    Chen, J.4
  • 16
    • 35848955628 scopus 로고    scopus 로고
    • Artemisinins and synthetic trioxolanes in the treatment of helminth infections
    • [16] Keiser, J., Utzinger, J., Artemisinins and synthetic trioxolanes in the treatment of helminth infections. Curr. Opin. Infect. Dis. 20 (2007), 605–612.
    • (2007) Curr. Opin. Infect. Dis. , vol.20 , pp. 605-612
    • Keiser, J.1    Utzinger, J.2
  • 17
    • 54249153209 scopus 로고    scopus 로고
    • A randomized, double-blind, placebo-controlled trial of safety and efficacy of combined praziquantel and artemether treatment for acute schistosomiasis japonica in China
    • [17] Hou, X.Y., McManus, D.P., Gray, D.J., Balen, J., Luo, X.S., He, Y.K., Ellis, M., Williams, G.M., Li, Y.S., A randomized, double-blind, placebo-controlled trial of safety and efficacy of combined praziquantel and artemether treatment for acute schistosomiasis japonica in China. Bull. World Health Organ. 86 (2008), 788–795.
    • (2008) Bull. World Health Organ. , vol.86 , pp. 788-795
    • Hou, X.Y.1    McManus, D.P.2    Gray, D.J.3    Balen, J.4    Luo, X.S.5    He, Y.K.6    Ellis, M.7    Williams, G.M.8    Li, Y.S.9
  • 18
    • 0036103409 scopus 로고    scopus 로고
    • Recent investigations of artemether, a novel agent for the prevention of schistosomiasis japonica, mansoni and haematobia
    • [18] Xiao, S., Tanner, M., N'Goran, E.K., Utzinger, J., Chollet, J., Bergquist, R., Chen, M., Zheng, J., Recent investigations of artemether, a novel agent for the prevention of schistosomiasis japonica, mansoni and haematobia. Acta Trop. 82 (2002), 175–181.
    • (2002) Acta Trop. , vol.82 , pp. 175-181
    • Xiao, S.1    Tanner, M.2    N'Goran, E.K.3    Utzinger, J.4    Chollet, J.5    Bergquist, R.6    Chen, M.7    Zheng, J.8
  • 19
    • 84861225927 scopus 로고    scopus 로고
    • Comparative studies on the interactions of honokiol and magnolol with human serum albumin
    • [19] Cheng, Z.J., Comparative studies on the interactions of honokiol and magnolol with human serum albumin. J. Pharmaceut. Biomed. Anal. 66 (2012), 240–251.
    • (2012) J. Pharmaceut. Biomed. Anal. , vol.66 , pp. 240-251
    • Cheng, Z.J.1
  • 20
    • 0003422992 scopus 로고    scopus 로고
    • Exploring Chemistry with Electronic Structure Methods
    • second ed. Gaussian Inc. Pittsburgh, PA, USA
    • [20] Foresman, J.B., Frisch, A., Exploring Chemistry with Electronic Structure Methods. second ed., 1996, Gaussian Inc., Pittsburgh, PA, USA.
    • (1996)
    • Foresman, J.B.1    Frisch, A.2
  • 21
    • 77953865084 scopus 로고    scopus 로고
    • Principles of Fluorescence Spectroscopy
    • third ed. Springer
    • [21] Lakowicz, J.R., Principles of Fluorescence Spectroscopy. third ed., 278, 2006, Springer.
    • (2006) , vol.278
    • Lakowicz, J.R.1
  • 22
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process
    • [22] Ware, W.R., Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process. J. Phys. Chem. 66 (1962), 455–458.
    • (1962) J. Phys. Chem. , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 23
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules
    • [23] Lakowicz, J.R., Weber, G., Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules. Biochemistry 12 (1973), 4161–4170.
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.R.1    Weber, G.2
  • 24
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reaction: forces contributing to stability
    • [24] Ross, P.D., Subramanian, S., Thermodynamics of protein association reaction: forces contributing to stability. Biochemistry 20 (1981), 3096–3102.
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 25
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • [25] Sreerama, N., Woody, R.W., A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209 (1993), 32–44.
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 27
    • 84896445000 scopus 로고    scopus 로고
    • A combined spectroscopic and molecular docking study on site selective binding interaction of toluidine blue O with human and bovine serum albumins
    • [27] SelvaSharma, A., Anandakumar, S., Ilanchelian, M., A combined spectroscopic and molecular docking study on site selective binding interaction of toluidine blue O with human and bovine serum albumins. J. Lumin. 151 (2014), 206–218.
    • (2014) J. Lumin. , vol.151 , pp. 206-218
    • SelvaSharma, A.1    Anandakumar, S.2    Ilanchelian, M.3
  • 28
    • 84894514957 scopus 로고    scopus 로고
    • Investigation on the interaction of pyrene with bovine serum albumin using spectroscopic methods
    • [28] Xu, C.B., Gu, J.L., Ma, X.P., Dong, T., Meng, X.L., Investigation on the interaction of pyrene with bovine serum albumin using spectroscopic methods. Spectrochim. Acta A 125 (2014), 391–395.
    • (2014) Spectrochim. Acta A , vol.125 , pp. 391-395
    • Xu, C.B.1    Gu, J.L.2    Ma, X.P.3    Dong, T.4    Meng, X.L.5
  • 29
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • [29] Surewicz, W.K., Mantsch, H.H., New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta Protein Proteomics 952 (1988), 115–130.
    • (1988) Biochim. Biophys. Acta Protein Proteomics , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 30
    • 84908137075 scopus 로고    scopus 로고
    • The secondary and aggregation structural changes of BSA induced by trivalent chromium: a biophysical study
    • [30] Chen, M., Liu, Y., Cao, H., Song, L., Zhang, Q., The secondary and aggregation structural changes of BSA induced by trivalent chromium: a biophysical study. J. Lumin. 158 (2015), 116–124.
    • (2015) J. Lumin. , vol.158 , pp. 116-124
    • Chen, M.1    Liu, Y.2    Cao, H.3    Song, L.4    Zhang, Q.5
  • 32
    • 84884298959 scopus 로고    scopus 로고
    • The investigation of the interaction between Tropicamide and bovine serum albumin by spectroscopic methods
    • [32] Yu, X.Y., Liao, Z.L., Yao, Q., Liu, H., Li, X.F., Yi, P.G., The investigation of the interaction between Tropicamide and bovine serum albumin by spectroscopic methods. Spectrochim. Acta A 118 (2014), 331–336.
    • (2014) Spectrochim. Acta A , vol.118 , pp. 331-336
    • Yu, X.Y.1    Liao, Z.L.2    Yao, Q.3    Liu, H.4    Li, X.F.5    Yi, P.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.