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Volumn 4, Issue , 2014, Pages

Atomic force microscopy based nanoassay: A new method to study α-Synuclein-dopamine bioaffinity interactions

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; DOPAMINE; GOLD; METAL NANOPARTICLE; PROTEIN BINDING;

EID: 84903190125     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep05366     Document Type: Article
Times cited : (10)

References (35)
  • 1
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • DOI 10.1038/35081564
    • Goedert, M. Alpha-synuclein and neurodegenerative diseases. Nat. Rev. Neurosci. 2, 492-501 (2001). (Pubitemid 33676584)
    • (2001) Nature Reviews Neuroscience , vol.2 , Issue.7 , pp. 492-501
    • Goedert, M.1
  • 2
    • 33750284754 scopus 로고    scopus 로고
    • Interaction of alpha-synuclein and dopamine metabolites in the pathogenesis of Parkinson's disease: A case for the selective vulnerability of the substantia nigra
    • Galvin, J. E. Interaction of alpha-synuclein and dopamine metabolites in the pathogenesis of Parkinson's disease: a case for the selective vulnerability of the substantia nigra. Acta Neuropathol. 112, 115-26 (2006).
    • (2006) Acta Neuropathol , vol.112 , pp. 115-126
    • Galvin, J.E.1
  • 3
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the α-synuclein protofibril by a dopamine-α-synuclein adduct
    • DOI 10.1126/science.1063522
    • Conway, K. a., Rochet, J. C., Bieganski, R. M. & Lansbury, P. T. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294, 1346-9 (2001). (Pubitemid 33063102)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.-C.2    Bieganski, R.M.3    Lansbury Jr., P.T.4
  • 4
    • 0031013141 scopus 로고    scopus 로고
    • Apoptotic-like changes in Lewy-body-associated disorders and normal aging in substantia nigral neurons
    • Tompkins, M. M., Basgall, E. J., Zamrini, E. & Hill, W. D. Apoptotic-like changes in Lewy-body-associated disorders and normal aging in substantia nigral neurons. Am. J. Pathol. 150, 119-31 (1997). (Pubitemid 27027103)
    • (1997) American Journal of Pathology , vol.150 , Issue.1 , pp. 119-131
    • Tompkins, M.M.1    Basgall, E.J.2    Zamrini, E.3    Hill, W.D.4
  • 5
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nat
    • Goldberg, M. S. & Lansbury Jr, P. T. Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nat. Cell Biol. 2, E115-E119 (2000).
    • (2000) Cell Biol. , vol.2
    • Goldberg, M.S.1    Lansbury Jr., P.T.2
  • 6
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • DOI 10.1021/bi991447r
    • Conway, K. A.,Harper, J. D.&Lansbury, P. T. Fibrils Formed in Vitro from alpha-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical Amyloid. Biochemistry 39, 2552-2563 (2000). (Pubitemid 30148907)
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury Jr., P.T.3
  • 7
    • 38849174979 scopus 로고    scopus 로고
    • Dopamine-modified a-synuclein blocks chaperonemediated autophagy
    • Martinez-Vicente, M. et al. Dopamine-modified a-synuclein blocks chaperonemediated autophagy. J. Clin. Invest. 118, 777-788 (2008).
    • (2008) J. Clin. Invest. , vol.118 , pp. 777-788
    • Martinez-Vicente, M.1
  • 11
    • 0034669882 scopus 로고    scopus 로고
    • Why are natively unfolded proteins unstructured under physiologic conditions?
    • Uversky, V. N., Gillespie, J. R. & Finka L. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41, 415-27 (2000).
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Finka, L.3
  • 12
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alphasynuclein secondary structure upon binding to synthetic membranes
    • Davidson, W. S., Jonas, a., Clayton, D. F. & George, J. M. Stabilization of alphasynuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 273, 9443-9 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 13
    • 84857649648 scopus 로고    scopus 로고
    • And misfolding of alpha-synuclein on membranes
    • Dikiy, I. & Eliezer, D. Folding and misfolding of alpha-synuclein on membranes. Biochim. Biophys. Acta 1818, 1013-8 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1013-1018
    • Dikiy, I.1    Folding, E.D.2
  • 14
    • 47249110199 scopus 로고    scopus 로고
    • The fold of a-synuclein fibrils
    • Vilar, M. et al. The fold of a-synuclein fibrils. Proc. Natl. Acad. Sci. 105, 8637-8642 (2008).
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 8637-8642
    • Vilar, M.1
  • 15
    • 28844441969 scopus 로고    scopus 로고
    • Secondary structure of α-synuclein oligomers: Characterization by Raman and atomic force microscopy
    • DOI 10.1016/j.jmb.2005.10.071, PII S0022283605013318
    • Apetri, M. M., Maiti, N. C., Zagorski, M. G., Carey, P. R. & Anderson, V. E. Secondary structure of alpha-synuclein oligomers: characterization by raman and atomic force microscopy. J. Mol. Biol. 355, 63-71 (2006). (Pubitemid 41774139)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.1 , pp. 63-71
    • Apetri, M.M.1    Maiti, N.C.2    Zagorski, M.G.3    Carey, P.R.4    Anderson, V.E.5
  • 16
    • 30344440844 scopus 로고    scopus 로고
    • Characterization of surface-confined α-synuclein by surface plasmon resonance measurements
    • DOI 10.1021/la052276w
    • Kang, T. et al. Characterization of surface-confined alpha-synuclein by surface plasmon resonance measurements. Langmuir 22, 13-7 (2006). (Pubitemid 43063515)
    • (2006) Langmuir , vol.22 , Issue.1 , pp. 13-17
    • Kang, T.1    Hong, S.2    Kim, H.J.3    Moon, J.4    Oh, S.5    Paik, S.R.6    Yi, J.7
  • 17
    • 38049072194 scopus 로고    scopus 로고
    • A more efficient enzyme-linked immunosorbent assay for measurement of alpha-synuclein in cerebrospinal fluid
    • Van Geel, W. J. A. et al. A more efficient enzyme-linked immunosorbent assay for measurement of alpha-synuclein in cerebrospinal fluid. J. Neurosci. Methods 168, 182-185 (2008).
    • (2008) J. Neurosci. Methods , vol.168 , pp. 182-185
    • Van Geel, W.J.A.1
  • 18
    • 78651257356 scopus 로고    scopus 로고
    • A photoelectrochemical immunosensor based on au-doped TiO2 nanotube arrays for the detection of a-synuclein
    • An, Y. et al. A photoelectrochemical immunosensor based on au-doped TiO2 nanotube arrays for the detection of a-synuclein. Chem.-A Eur. J. 16, 14439-14446 (2010).
    • (2010) Chem.-A Eur. J. , vol.16 , pp. 14439-14446
    • An, Y.1
  • 20
    • 0035807149 scopus 로고    scopus 로고
    • A survey of structure-property relationships of surfaces that resist the adsorption of protein
    • DOI 10.1021/la010384m
    • Ostuni, E., Chapman, R. G., Holmlin, R. E., Takayama, S. & Whitesides, G. M. A survey of structure-property relationships of surfaces that resist the adsorption of protein. Langmuir 17, 5605-5620 (2001). (Pubitemid 35330800)
    • (2001) Langmuir , vol.17 , Issue.18 , pp. 5605-5620
    • Ostuni, E.1    Chapman, R.G.2    Holmlin, R.E.3    Takayama, S.4    Whitesides, G.M.5
  • 21
    • 43949111654 scopus 로고    scopus 로고
    • Nanografting for surface physical chemistry
    • DOI 10.1146/annurev.physchem.58.032806.104542
    • Liu,M., Amro, N. A. & Liu, G. Nanografting for surface physical chemistry. Annu. Rev. Phys. Chem. 59, 367-386 (2008). (Pubitemid 351703391)
    • (2008) Annual Review of Physical Chemistry , vol.59 , pp. 367-386
    • Liu, M.1    Amro, N.A.2    Liu, G.-Y.3
  • 22
    • 52049114136 scopus 로고    scopus 로고
    • Ligand-induced structural changes in maltose binding proteins measured by atomic force microscopy
    • Staii, C., Wood, D. & Scoles, G. Ligand-induced structural changes in maltose binding proteins measured by atomic force microscopy. Nano Lett. 8, 2503-2509 (2008).
    • (2008) Nano Lett. , vol.8 , pp. 2503-2509
    • Staii, C.1    Wood, D.2    Scoles, G.3
  • 23
    • 67650361634 scopus 로고    scopus 로고
    • Toward multiprotein nanoarrays using nanografting and DNA directed immobilization of proteins
    • Bano, F. et al. Toward multiprotein nanoarrays using nanografting and DNA directed immobilization of proteins. Nano Lett. 9, 2614-18 (2009).
    • (2009) Nano Lett. , vol.9 , pp. 2614-2618
    • Bano, F.1
  • 24
    • 78649613243 scopus 로고    scopus 로고
    • Oriented immobilization of prion protein demonstrated via precise interfacial nanostructure measurements
    • Sanavio, B. et al. Oriented immobilization of prion protein demonstrated via precise interfacial nanostructure measurements. ACS Nano 4, 6607-16 (2010).
    • (2010) ACS Nano , vol.4 , pp. 6607-6616
    • Sanavio, B.1
  • 25
    • 61649123047 scopus 로고    scopus 로고
    • Quantitative Study of the Effect of Coverage on the Hybridization Efficiency of Surface-Bound DNA Nanostructures
    • Mirmomtaz, E. et al. Quantitative Study of the Effect of Coverage on the Hybridization Efficiency of Surface-Bound DNA Nanostructures. Nano 8, 4134-4139 (2008).
    • (2008) Nano , vol.8 , pp. 4134-4139
    • Mirmomtaz, E.1
  • 26
    • 0037432332 scopus 로고    scopus 로고
    • Conformational behavior and aggregation of α-synuclein in organic solvents: Modeling the effects of membranes
    • DOI 10.1021/bi027166s
    • Munishkina, L. A., Phelan, C., Uversky, V. N. & Fink, A. L. Conformational behavior and aggregation of a-synuclein in organic solvents: Modeling the effects of membranes. Biochemistry 42, 2720-2730 (2003). (Pubitemid 36330626)
    • (2003) Biochemistry , vol.42 , Issue.9 , pp. 2720-2730
    • Munishkina, L.A.1    Phelan, C.2    Uversky, V.N.3    Fink, A.L.4
  • 27
    • 78650505110 scopus 로고    scopus 로고
    • Identification of a helical intermediate in trifluoroethanol-induced alphasynuclein aggregation
    • Anderson, V. L., Ramlall, T. F., Rospigliosi, C. C., Webb, W. W. & Eliezer, D. Identification of a helical intermediate in trifluoroethanol-induced alphasynuclein aggregation. PNAS 107, 18850-18855 (2010).
    • (2010) PNAS , vol.107 , pp. 18850-18855
    • Anderson, V.L.1    Ramlall, T.F.2    Rospigliosi, C.C.3    Webb, W.W.4    Eliezer, D.5
  • 28
    • 77950659588 scopus 로고    scopus 로고
    • Early aggregation steps in alpha-synuclein as measured by FCS and FRET: Evidence for a contagious conformational change
    • Nath, S., Meuvis, J., Hendrix, J., Carl, S. a. & Engelborghs, Y. Early aggregation steps in alpha-synuclein as measured by FCS and FRET: evidence for a contagious conformational change. Biophys. J. 98, 1302-11 (2010).
    • (2010) Biophys. J. , vol.98 , pp. 1302-1311
    • Nath, S.1    Meuvis, J.2    Hendrix, J.3    Carl, S.A.4    Engelborghs, Y.5
  • 29
    • 0034651575 scopus 로고    scopus 로고
    • A panel of epitope-specific antibodies detects protein domains distributed throughout human α-synuclein in Lewy bodies of Parkinson's disease
    • DOI 10.1002/(SICI)1097-4547(20000215) 59:4<528::AID-JNR8>3.0.CO;2-0
    • Giasson, B. I. et al. A panel of epitope-specific antibodies detects protein domains distributed throughout human alpha-synuclein in Lewy bodies of Parkinson's disease. J. Neurosci. Res. 59, 528-533 (2000). (Pubitemid 30090580)
    • (2000) Journal of Neuroscience Research , vol.59 , Issue.4 , pp. 528-533
    • Giasson, B.I.1    Jakes, R.2    Goedert, M.3    Duda, J.E.4    Leight, S.5    Trojanowski, J.Q.6    Lee, V.M.Y.7
  • 30
    • 33646112656 scopus 로고    scopus 로고
    • Comparative study of commercially available anti-alphasynuclein antibodies
    • Croisier, E. et al. Comparative study of commercially available anti-alphasynuclein antibodies. Neuropathol. Appl. Neurobiol. 32, 351-356 (2006).
    • (2006) Neuropathol. Appl. Neurobiol. , vol.32 , pp. 351-356
    • Croisier, E.1
  • 31
    • 54849423681 scopus 로고    scopus 로고
    • Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region
    • Herrera, F. E. et al. Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region. PLoS One 3, e3394 (2008).
    • (2008) PLoS One , vol.3
    • Herrera, F.E.1
  • 32
    • 84884825977 scopus 로고    scopus 로고
    • A molecular dynamics simulation-based interpretation of nuclear magnetic resonance multidimensional heteronuclear spectra of a-synuclein?dopamine adducts
    • Dibenedetto, D., Rossetti, G., Caliandro, R. & Carloni, P. A molecular dynamics simulation-based interpretation of nuclear magnetic resonance multidimensional heteronuclear spectra of a-synuclein?dopamine adducts. Biochemistry 52, 6672-83 (2013).
    • (2013) Biochemistry , vol.52 , pp. 6672-6683
    • Dibenedetto, D.1    Rossetti, G.2    Caliandro, R.3    Carloni, P.4
  • 33
    • 0027625621 scopus 로고
    • Ultralarge atomically flat templatestripped Au surfaces for scanning probe microscopy
    • Hegner, M., Wagner, P. & Semenza, G. Ultralarge atomically flat templatestripped Au surfaces for scanning probe microscopy. Surf. Sci. 291, 39-46 (1993).
    • (1993) Surf. Sci. , vol.291 , pp. 39-46
    • Hegner, M.1    Wagner, P.2    Semenza, G.3
  • 34
    • 78049310914 scopus 로고    scopus 로고
    • The conformation and the aggregation kinetics of a-Synuclein depend on the proline residues in Its C-terminal region
    • Meuvis, J., Gerard, M., Desender, L., Baekelandt, V. & Engelborghs, Y. The conformation and the aggregation kinetics of a-Synuclein depend on the proline residues in Its C-terminal region. Biochemistry 49, 9345-9352 (2010).
    • (2010) Biochemistry , vol.49 , pp. 9345-9352
    • Meuvis, J.1    Gerard, M.2    Desender, L.3    Baekelandt, V.4    Engelborghs, Y.5


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