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Volumn 25, Issue 6, 2015, Pages 1567-1575

A Note on the use of Steady-State Fluorescence Quenching to Quantify Nanoparticle-Protein Interactions

Author keywords

Fluorescence quenching; Gold nanoparticles; Hill equation; Protein adsorption; Spectroscopic titration

Indexed keywords

BINDING ENERGY; BINS; BIOCHEMISTRY; FLUORESCENCE; NANOPARTICLES; PROTEINS;

EID: 84946922971     PISSN: 10530509     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10895-015-1665-3     Document Type: Article
Times cited : (29)

References (37)
  • 1
    • 84864741149 scopus 로고    scopus 로고
    • Toward a molecular understanding of nanoparticle-protein interactions
    • 1:CAS:528:DC%2BC38XmvFahtbg%3D
    • Treuel L, Nienhaus GU (2012) Toward a molecular understanding of nanoparticle-protein interactions. Biophys Rev 4:137-147
    • (2012) Biophys Rev , vol.4 , pp. 137-147
    • Treuel, L.1    Nienhaus, G.U.2
  • 2
    • 33847789142 scopus 로고    scopus 로고
    • Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles
    • 1892985 1:CAS:528:DC%2BD2sXisVWrsro%3D 17267609
    • Cedervall T, Lynch I, Lindman S, Berggård T, Thulin E, Nilsson H, Dawson KA, Linse S (2007) Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci U S A 104:2050-2055
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 2050-2055
    • Cedervall, T.1    Lynch, I.2    Lindman, S.3    Berggård, T.4    Thulin, E.5    Nilsson, H.6    Dawson, K.A.7    Linse, S.8
  • 3
    • 84892514307 scopus 로고    scopus 로고
    • 25th anniversary article: Interfacing nanoparticles and biology: New strategies for biomedicine
    • 4067239 1:CAS:528:DC%2BC3sXhsF2ntb3P 24105763
    • Tonga GY, Saha K, Rotello VM (2014) 25th anniversary article: interfacing nanoparticles and biology: new strategies for biomedicine. Adv Mater 26:359-370
    • (2014) Adv Mater , vol.26 , pp. 359-370
    • Tonga, G.Y.1    Saha, K.2    Rotello, V.M.3
  • 4
    • 84946714654 scopus 로고    scopus 로고
    • Protein corona formation around nanoparticles - From the past to the future
    • Pd P, Pelaz B, Zhang Q, Maffre P, Nienhaus GU, Parak WJ (2014) Protein corona formation around nanoparticles - from the past to the future. Mater Horiz 1:301-313
    • (2014) Mater Horiz , vol.1 , pp. 301-313
    • Pd, P.1    Pelaz, B.2    Zhang, Q.3    Maffre, P.4    Nienhaus, G.U.5    Parak, W.J.6
  • 5
    • 84866518269 scopus 로고    scopus 로고
    • Systematically investigations of conformation and thermodynamics of HSA adsorbed to different sizes of CdTe quantum dots
    • 1:CAS:528:DC%2BC38XhslOltLbI 23006555
    • Xiao Q, Huang S, Su W, Li P, Ma J, Luo F, Chen J, Liu Y (2013) Systematically investigations of conformation and thermodynamics of HSA adsorbed to different sizes of CdTe quantum dots. Colloids Surf B: Biointerfaces 102:76-82
    • (2013) Colloids Surf B: Biointerfaces , vol.102 , pp. 76-82
    • Xiao, Q.1    Huang, S.2    Su, W.3    Li, P.4    Ma, J.5    Luo, F.6    Chen, J.7    Liu, Y.8
  • 6
    • 55749089574 scopus 로고    scopus 로고
    • Study on the interaction between bovine serum albumin and CdTe quantum dots with spectroscopic techniques
    • 1:CAS:528:DC%2BD1cXhsVSgur%2FM
    • Liang J, Cheng Y, Han H (2008) Study on the interaction between bovine serum albumin and CdTe quantum dots with spectroscopic techniques. J Mol Struct 892:116-120
    • (2008) J Mol Struct , vol.892 , pp. 116-120
    • Liang, J.1    Cheng, Y.2    Han, H.3
  • 7
    • 67349182612 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction of colloidal capped CdS nanoparticles with bovine serum albumin
    • Jhonsi MA, Kathiravan A, Renganathan R (2009) Spectroscopic studies on the interaction of colloidal capped CdS nanoparticles with bovine serum albumin. Colloids Surf B: Biointerfaces 72:167-172
    • (2009) Colloids Surf B: Biointerfaces , vol.72 , pp. 167-172
    • Jhonsi, M.A.1    Kathiravan, A.2    Renganathan, R.3
  • 8
    • 84865747005 scopus 로고    scopus 로고
    • Ultrasmall fluorescent silver nanoclusters: Protein adsorption and its effects on cellular responses
    • 1:CAS:528:DC%2BC38XhtFOntb%2FL
    • Shang L, Dörlich RM, Trouillet V, Bruns M, Nienhaus GU (2012) Ultrasmall fluorescent silver nanoclusters: protein adsorption and its effects on cellular responses. Nano Res 5:531-542
    • (2012) Nano Res , vol.5 , pp. 531-542
    • Shang, L.1    Dörlich, R.M.2    Trouillet, V.3    Bruns, M.4    Nienhaus, G.U.5
  • 10
    • 84889036006 scopus 로고    scopus 로고
    • Nanoparticle - Protein interactions: A thermodynamic and kinetic study of the adsorption of bovine serum albumin to gold nanoparticle surfaces
    • 1:CAS:528:DC%2BC3sXhslGgs73J 24215427
    • Boulos SP, Davis TA, Yang JA, Lohse SE, Alkilany AM, Holland LA, Murphy CJ (2013) Nanoparticle - protein interactions: a thermodynamic and kinetic study of the adsorption of bovine serum albumin to gold nanoparticle surfaces. Langmuir 29:14984-14996
    • (2013) Langmuir , vol.29 , pp. 14984-14996
    • Boulos, S.P.1    Davis, T.A.2    Yang, J.A.3    Lohse, S.E.4    Alkilany, A.M.5    Holland, L.A.6    Murphy, C.J.7
  • 11
    • 84875968263 scopus 로고    scopus 로고
    • Study of wild-type α-synuclein binding and orientation on gold nanoparticles
    • 1:CAS:528:DC%2BC3sXjslGhtLo%3D 23477540
    • Yang JA, Johnson BJ, Wu S, Woods WS, George JM, Murphy CJ (2013) Study of wild-type α-synuclein binding and orientation on gold nanoparticles. Langmuir 29:4603-4615
    • (2013) Langmuir , vol.29 , pp. 4603-4615
    • Yang, J.A.1    Johnson, B.J.2    Wu, S.3    Woods, W.S.4    George, J.M.5    Murphy, C.J.6
  • 14
    • 0035229342 scopus 로고    scopus 로고
    • Analysis of DNA-protein interactions by intrinsic fluorescence
    • 1:CAS:528:DC%2BD3MXivV2nsLw%3D 11357608
    • Carpenter ML, Oliver AW, Kneale GG (2001) Analysis of DNA-protein interactions by intrinsic fluorescence. Methods Mol Biol 148:491-502
    • (2001) Methods Mol Biol , vol.148 , pp. 491-502
    • Carpenter, M.L.1    Oliver, A.W.2    Kneale, G.G.3
  • 15
    • 78650949718 scopus 로고    scopus 로고
    • Measurement and analysis of equilibrium binding titrations: A beginner's guide
    • 1:CAS:528:DC%2BC3MXjt1Sks7s%3D 21195222
    • Beckett D (2011) Measurement and analysis of equilibrium binding titrations: a beginner's guide. Methods Enzymol 488:1-16
    • (2011) Methods Enzymol , vol.488 , pp. 1-16
    • Beckett, D.1
  • 16
    • 80052970305 scopus 로고    scopus 로고
    • On the evaluation of the number of binding sites in proteins from steady state fluorescence measurements
    • 1:CAS:528:DC%2BC3MXhtVynsrbF 21484310
    • Lissi E, Abuin E (2011) On the evaluation of the number of binding sites in proteins from steady state fluorescence measurements. J Fluoresc 21:1831-1833
    • (2011) J Fluoresc , vol.21 , pp. 1831-1833
    • Lissi, E.1    Abuin, E.2
  • 17
    • 84907677832 scopus 로고    scopus 로고
    • Quantitative thermodynamic analyses of spectroscopic titration curves
    • 1:CAS:528:DC%2BC2cXnslWgs7Y%3D 25284889
    • Bujalowski W, Jezewska MJ (2014) Quantitative thermodynamic analyses of spectroscopic titration curves. J Mol Struct 1077:40-50
    • (2014) J Mol Struct , vol.1077 , pp. 40-50
    • Bujalowski, W.1    Jezewska, M.J.2
  • 18
    • 77950865952 scopus 로고    scopus 로고
    • Fluorescence quenching to study protein-ligand binding: Common errors
    • Mvd W (2010) Fluorescence quenching to study protein-ligand binding: common errors. J Fluoresc 20:625-629
    • (2010) J Fluoresc , vol.20 , pp. 625-629
    • Mvd, W.1
  • 19
    • 79959690715 scopus 로고    scopus 로고
    • Fluorescence quenching and ligand binding: A critical discussion of a popular methodology
    • Mvd W, Stella L (2011) Fluorescence quenching and ligand binding: a critical discussion of a popular methodology. J Mol Struct 998:144-150
    • (2011) J Mol Struct , vol.998 , pp. 144-150
    • Mvd, W.1    Stella, L.2
  • 20
    • 84907621081 scopus 로고    scopus 로고
    • Fluorescence spectroscopy and binding: Getting it right
    • 1:CAS:528:DC%2BC2cXovVahtbw%3D
    • Stella L, Mvd W, Burrows HD, Fausto R (2014) Fluorescence spectroscopy and binding: getting it right. J Mol Struct 1077:1-3
    • (2014) J Mol Struct , vol.1077 , pp. 1-3
    • Stella, L.1    Mvd, W.2    Burrows, H.D.3    Fausto, R.4
  • 21
    • 0034496256 scopus 로고    scopus 로고
    • A note on the analysis of ligand binding by the 'double-logarithmic' plot
    • 1:CAS:528:DC%2BD3MXhtFartLc%3D 11233647
    • Grossweiner LI (2000) A note on the analysis of ligand binding by the 'double-logarithmic' plot. J Photochem Photobiol B: Biology 58:175-177
    • (2000) J Photochem Photobiol B: Biology , vol.58 , pp. 175-177
    • Grossweiner, L.I.1
  • 22
    • 84887403944 scopus 로고    scopus 로고
    • Evaluation of the number of binding sites in proteins from their intrinsic fluorescence: Limitations and pitfalls
    • 1:CAS:528:DC%2BC3sXhslWntLbF 23789593
    • Lissi E, Calderon C, Campos A (2013) Evaluation of the number of binding sites in proteins from their intrinsic fluorescence: limitations and pitfalls. Photochem Photobiol 89:1413-1416
    • (2013) Photochem Photobiol , vol.89 , pp. 1413-1416
    • Lissi, E.1    Calderon, C.2    Campos, A.3
  • 23
    • 54749112200 scopus 로고    scopus 로고
    • A reassessment of the association between azulene and [60]fullerene. Possible pitfalls in the determination of binding constants through fluorescence spectroscopy
    • Stella L, Capodilupo AL, Bietti M (2008) A reassessment of the association between azulene and [60]fullerene. Possible pitfalls in the determination of binding constants through fluorescence spectroscopy. Chem Commun (39):4744-4746
    • (2008) Chem Commun , vol.39 , pp. 4744-4746
    • Stella, L.1    Capodilupo, A.L.2    Bietti, M.3
  • 24
    • 0023229226 scopus 로고
    • A general method of analysis of ligand-macromolecule equilibria using a spectroscopic signal from the ligand to monitor binding. Application to Escherichia coli Single-Strand Binding Protein-Nucleic Acid Interactions
    • 1:CAS:528:DyaL2sXitFSgsbo%3D 3300771
    • Bujalowski W, Lohman TM (1987) A general method of analysis of ligand-macromolecule equilibria using a spectroscopic signal from the ligand to monitor binding. Application to Escherichia coli Single-Strand Binding Protein-Nucleic Acid Interactions. Biochemistry 26:3099-3106
    • (1987) Biochemistry , vol.26 , pp. 3099-3106
    • Bujalowski, W.1    Lohman, T.M.2
  • 25
    • 33644632662 scopus 로고    scopus 로고
    • Thermodynamic and kinetic methods of analyses of protein - Nucleic acid interactions. from Simpler to More Complex Systems
    • 1:CAS:528:DC%2BD28XoslGrtQ%3D%3D
    • Bujalowski W (2006) Thermodynamic and kinetic methods of analyses of protein - nucleic acid interactions. From Simpler to More Complex Systems. Biochemistry 106:556-606
    • (2006) Biochemistry , vol.106 , pp. 556-606
    • Bujalowski, W.1
  • 26
    • 0034734301 scopus 로고    scopus 로고
    • A universal thermodynamic approach to analyze biomolecular binding experiments
    • 1:CAS:528:DC%2BD3cXlvV2ksbs%3D 11026677
    • Schwarz G (2000) A universal thermodynamic approach to analyze biomolecular binding experiments. Biophys Chem 86:119-129
    • (2000) Biophys Chem , vol.86 , pp. 119-129
    • Schwarz, G.1
  • 27
    • 84946899356 scopus 로고    scopus 로고
    • Multiple equilibria
    • H. Bisswanger (eds) 2nd Wiley-VCH Verlag GmbH & Co. KGaA Weinheim
    • Bisswanger H (2008) Multiple equilibria. In: Bisswanger H (ed) Enzyme kinetics: principles and methods, 2nd edn. Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, pp. 7-58
    • (2008) Enzyme Kinetics: Principles and Methods , pp. 7-58
    • Bisswanger, H.1
  • 28
    • 0001314221 scopus 로고
    • The hemoglobin system. The Oxygen dissociation Curve of Haemoglobin
    • 1:CAS:528:DyaB2MXhslSiug%3D%3D
    • Adair GS (1925) The hemoglobin system. The Oxygen dissociation Curve of Haemoglobin. J Biol Chem 63:529-545
    • (1925) J Biol Chem , vol.63 , pp. 529-545
    • Adair, G.S.1
  • 29
    • 84927602021 scopus 로고    scopus 로고
    • A generalized model on the effects of nanoparticles on fluorophore fluorescence in solution
    • 1:CAS:528:DC%2BC2MXksFSrsbw%3D
    • Zhang D, Nettles CB (2015) A generalized model on the effects of nanoparticles on fluorophore fluorescence in solution. J Phys Chem C 119:7941-7948
    • (2015) J Phys Chem C , vol.119 , pp. 7941-7948
    • Zhang, D.1    Nettles, C.B.2
  • 30
    • 84907657183 scopus 로고    scopus 로고
    • Inner filter effects and other traps in quantitative spectrofluorimetric measurements: Origins and methods of correction
    • 1:CAS:528:DC%2BC2cXmtFWisbk%3D
    • Credi A, Prodi L (2014) Inner filter effects and other traps in quantitative spectrofluorimetric measurements: origins and methods of correction. J Mol Struct 1077:30-39
    • (2014) J Mol Struct , vol.1077 , pp. 30-39
    • Credi, A.1    Prodi, L.2
  • 31
    • 84858054510 scopus 로고    scopus 로고
    • Effect of protein adsorption on the fluorescence of ultrasmall gold nanoclusters
    • 1:CAS:528:DC%2BC3MXhs12gsbzN 22213653
    • Shang L, Brandholt S, Stockmar F, Trouillet V, Bruns M, Nienhaus GU (2012) Effect of protein adsorption on the fluorescence of ultrasmall gold nanoclusters. Small 8:661-665
    • (2012) Small , vol.8 , pp. 661-665
    • Shang, L.1    Brandholt, S.2    Stockmar, F.3    Trouillet, V.4    Bruns, M.5    Nienhaus, G.U.6
  • 32
    • 77951677879 scopus 로고    scopus 로고
    • Gold nanoparticle-fluorophore complexes: Sensitive and discerning "noses" for biosystems sensing
    • Bunz UHF, Rotello VM (2010) Gold nanoparticle-fluorophore complexes: sensitive and discerning "noses" for biosystems sensing. Angew Chem Int Ed 39:3268-3279
    • (2010) Angew Chem Int Ed , vol.39 , pp. 3268-3279
    • Bunz, U.H.F.1    Rotello, V.M.2
  • 33
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • 1:CAS:528:DyaK28XjtlOktL4%3D 8660575
    • Kuzmic P (1996) Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal Biochem 237:260-273
    • (1996) Anal Biochem , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 34
    • 77957243218 scopus 로고    scopus 로고
    • Site-specific biomolecule labeling with gold clusters
    • 3568671 1:CAS:528:DC%2BC3cXhs1SisrbI 20887859
    • Ackerson CJ, Powell RD, Hainfeld JF (2010) Site-specific biomolecule labeling with gold clusters. Methods Enzymol 481:195-230
    • (2010) Methods Enzymol , vol.481 , pp. 195-230
    • Ackerson, C.J.1    Powell, R.D.2    Hainfeld, J.F.3
  • 35
    • 84864125079 scopus 로고    scopus 로고
    • Synthesis, characterization, and direct intracellular imaging of ultrasmall and uniform glutathione-coated gold nanoparticles
    • 3715615 1:CAS:528:DC%2BC38XlslyktLc%3D 22517616
    • Sousa AA, Morgan JT, Brown PH, Adams A, Jayasekara MPS, Zhang G, Ackerson CJ, Kruhlak MJ, Leapman RD (2012) Synthesis, characterization, and direct intracellular imaging of ultrasmall and uniform glutathione-coated gold nanoparticles. Small 8:2277-2286
    • (2012) Small , vol.8 , pp. 2277-2286
    • Sousa, A.A.1    Morgan, J.T.2    Brown, P.H.3    Adams, A.4    Jayasekara, M.P.S.5    Zhang, G.6    Ackerson, C.J.7    Kruhlak, M.J.8    Leapman, R.D.9
  • 37
    • 0034228033 scopus 로고    scopus 로고
    • Monolayer-protected clusters with fluorescent dansyl
    • 1:CAS:528:DC%2BD3cXktVagsLY%3D
    • Aguila A, Murray RW (2000) Monolayer-protected clusters with fluorescent dansyl. Langmuir 16:5949-5954
    • (2000) Langmuir , vol.16 , pp. 5949-5954
    • Aguila, A.1    Murray, R.W.2


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