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Volumn 29, Issue 50, 2013, Pages 15634-15642

Investigation of Cu2+ binding to human and rat amyloid fragments Aβ (1-16) with a protein nanopore

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID-BETA PEPTIDES; ASSOCIATION AND DISSOCIATION KINETICS; METAL COORDINATION; MORPHOLOGY CHANGES; PEPTIDE FRAGMENTS; PRIMARY SEQUENCES; REVERSIBLE INTERACTIONS; STRUCTURAL ALTERATIONS;

EID: 84890586010     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la403915t     Document Type: Article
Times cited : (42)

References (42)
  • 1
    • 0035855827 scopus 로고    scopus 로고
    • Stochastic Sensors Inspired by Biology
    • Bayley, H.; Cremer, P. S. Stochastic Sensors Inspired by Biology Nature 2001, 413, 226-230
    • (2001) Nature , vol.413 , pp. 226-230
    • Bayley, H.1    Cremer, P.S.2
  • 2
    • 77249128977 scopus 로고    scopus 로고
    • Single Molecule Sensing by Nanopores and Nanopore Devices
    • Gu, L.-Q.; Shim, J. W. Single Molecule Sensing by Nanopores and Nanopore Devices Analyst 2010, 135, 441-451
    • (2010) Analyst , vol.135 , pp. 441-451
    • Gu, L.-Q.1    Shim, J.W.2
  • 5
    • 0014813247 scopus 로고
    • Counting and Sizing of Submicron Particles by the Resistive Pulse Technique
    • DeBlois, R. W.; Bean, C. P. Counting and Sizing of Submicron Particles by the Resistive Pulse Technique Rev. Sci. Instrum. 1970, 41, 909-916
    • (1970) Rev. Sci. Instrum. , vol.41 , pp. 909-916
    • Deblois, R.W.1    Bean, C.P.2
  • 6
    • 78650688478 scopus 로고    scopus 로고
    • Investigation of Single-Molecule Kinetics Mediated by Weak Hydrogen-Bonds within a Biological Nanopore
    • Asandei, A.; Apetrei, A.; Park, Y.; Hahm, K.-S.; Luchian, T. Investigation of Single-Molecule Kinetics Mediated by Weak Hydrogen-Bonds within a Biological Nanopore Langmuir 2011, 27, 19-24
    • (2011) Langmuir , vol.27 , pp. 19-24
    • Asandei, A.1    Apetrei, A.2    Park, Y.3    Hahm, K.-S.4    Luchian, T.5
  • 7
    • 0037020426 scopus 로고    scopus 로고
    • Kinetics of a Reversible Covalent-Bond Forming Reaction Observed at the Single Molecule Level
    • Shin, S.-H.; Luchian, T.; Cheley, S.; Braha, O.; Bayley, H. Kinetics of a Reversible Covalent-Bond Forming Reaction Observed at the Single Molecule Level Angew. Chem., Int. Ed. 2002, 41, 3707-3709
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 3707-3709
    • Shin, S.-H.1    Luchian, T.2    Cheley, S.3    Braha, O.4    Bayley, H.5
  • 8
    • 84860393376 scopus 로고    scopus 로고
    • The Kinetics of Ampicillin Complexation by γ-Cyclodextrins. A Single Molecule Approach
    • Asandei, A.; Mereuta, L.; Luchian, T. The Kinetics of Ampicillin Complexation by γ-Cyclodextrins. A Single Molecule Approach J. Phys. Chem. B 2011, 115, 10173-10181
    • (2011) J. Phys. Chem. B , vol.115 , pp. 10173-10181
    • Asandei, A.1    Mereuta, L.2    Luchian, T.3
  • 9
    • 0033594410 scopus 로고    scopus 로고
    • Stochastic Sensing of Organic Analytes by a Pore-Forming Protein Containing a Molecular Adapter
    • Gu, L.-Q.; Braha, O.; Conlan, S.; Cheley, S.; Bayley, H. Stochastic Sensing of Organic Analytes by a Pore-Forming Protein Containing a Molecular Adapter Nature 1999, 398, 686-690
    • (1999) Nature , vol.398 , pp. 686-690
    • Gu, L.-Q.1    Braha, O.2    Conlan, S.3    Cheley, S.4    Bayley, H.5
  • 10
    • 64449088698 scopus 로고    scopus 로고
    • Continuous Base Identification for Single-Molecule Nanopore DNA Sequencing
    • Clarke, J.; Wu, H.; Jayasinghe, L.; Patel, A.; Reid, S.; Bayley, H. Continuous Base Identification for Single-Molecule Nanopore DNA Sequencing Nat. Nanotechnol. 2009, 4, 265-270
    • (2009) Nat. Nanotechnol. , vol.4 , pp. 265-270
    • Clarke, J.1    Wu, H.2    Jayasinghe, L.3    Patel, A.4    Reid, S.5    Bayley, H.6
  • 11
    • 79952151618 scopus 로고    scopus 로고
    • Nanopore Analysis of β-Amyloid Peptide Aggregation Transition Induced by Small Molecules
    • Wang, H.-Y.; Ying, Y.-L.; Li, Y.; Kraatz, H.-B.; Long, Y.-T. Nanopore Analysis of β-Amyloid Peptide Aggregation Transition Induced by Small Molecules Anal. Chem. 2011, 83, 1746-1752
    • (2011) Anal. Chem. , vol.83 , pp. 1746-1752
    • Wang, H.-Y.1    Ying, Y.-L.2    Li, Y.3    Kraatz, H.-B.4    Long, Y.-T.5
  • 12
    • 79952168688 scopus 로고    scopus 로고
    • Uni-molecular Detection and Quantification of Selected β-Lactam Antibiotics with a Hybrid α-Hemolysin Protein Pore
    • Asandei, A.; Apetrei, A.; Luchian, T. Uni-molecular Detection and Quantification of Selected β-Lactam Antibiotics with a Hybrid α-Hemolysin Protein Pore J. Mol. Recognit. 2011, 24, 199-207
    • (2011) J. Mol. Recognit. , vol.24 , pp. 199-207
    • Asandei, A.1    Apetrei, A.2    Luchian, T.3
  • 13
    • 79955619143 scopus 로고    scopus 로고
    • Enhanced Translocation of Poly(dt)45 through an α-Hemolysin Nanopore by Binding with Antibody
    • Ying, Y.-L.; Li, D.-W.; Li, Y.; Lee, J. S.; Long, Y.-T. Enhanced Translocation of Poly(dt)45 through an α-Hemolysin Nanopore by Binding with Antibody Chem. Commun. 2011, 47, 5690-5692
    • (2011) Chem. Commun. , vol.47 , pp. 5690-5692
    • Ying, Y.-L.1    Li, D.-W.2    Li, Y.3    Lee, J.S.4    Long, Y.-T.5
  • 15
    • 84866419795 scopus 로고    scopus 로고
    • Continuous Stochastic Detection of Amino Acid Enantiomers with a Protein Nanopore
    • Boersma, A. J.; Bayley, H. Continuous Stochastic Detection of Amino Acid Enantiomers with a Protein Nanopore Angew. Chem., Int. Ed. 2012, 51, 9606-9609
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 9606-9609
    • Boersma, A.J.1    Bayley, H.2
  • 16
    • 84862889466 scopus 로고    scopus 로고
    • Real-Time Stochastic Detection of Multiple Neurotransmitters with a Protein Nanopore
    • Boersma, A. J.; Brain, K. L.; Bayley, H. Real-Time Stochastic Detection of Multiple Neurotransmitters with a Protein Nanopore ACS Nano 2012, 6, 5304-5308
    • (2012) ACS Nano , vol.6 , pp. 5304-5308
    • Boersma, A.J.1    Brain, K.L.2    Bayley, H.3
  • 19
    • 84863470343 scopus 로고    scopus 로고
    • Nanopores: A Journey towards DNA Sequencing
    • Wanunu, M. Nanopores: A Journey towards DNA Sequencing Phys. Life Rev. 2012, 9, 125-158
    • (2012) Phys. Life Rev. , vol.9 , pp. 125-158
    • Wanunu, M.1
  • 20
    • 38849087309 scopus 로고    scopus 로고
    • Nanopore Analysis of a Small 86-Residue Protein
    • Stefureac, R.; Waldner, L.; Howard, S. P.; Lee, J. S. Nanopore Analysis of a Small 86-Residue Protein Small 2008, 4, 59-63
    • (2008) Small , vol.4 , pp. 59-63
    • Stefureac, R.1    Waldner, L.2    Howard, S.P.3    Lee, J.S.4
  • 21
    • 72949107606 scopus 로고    scopus 로고
    • Divalent Cations Induce a Compaction of Intrinsically Disordered Myelin Basic Protein
    • Baran, C.; Smith, G. S. T.; Bamm, V. V.; Harauz, G.; Lee, J. S. Divalent Cations Induce a Compaction of Intrinsically Disordered Myelin Basic Protein Biochem. Biophys. Res. Commun. 2010, 391, 224-229
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 224-229
    • Baran, C.1    Smith, G.S.T.2    Bamm, V.V.3    Harauz, G.4    Lee, J.S.5
  • 22
    • 84870927202 scopus 로고    scopus 로고
    • Protein Nanopore-Based, Single-Molecule Exploration of Copper Binding to an Antimicrobial-Derived, Histidine-Containing Chimera Peptide
    • Mereuta, L.; Schiopu, I.; Asandei, A.; Park, Y.; Hahm, K.-S.; Luchian, T. Protein Nanopore-Based, Single-Molecule Exploration of Copper Binding to an Antimicrobial-Derived, Histidine-Containing Chimera Peptide Langmuir 2012, 28, 17079-17091
    • (2012) Langmuir , vol.28 , pp. 17079-17091
    • Mereuta, L.1    Schiopu, I.2    Asandei, A.3    Park, Y.4    Hahm, K.-S.5    Luchian, T.6
  • 23
    • 77955312210 scopus 로고    scopus 로고
    • Amyloidogenic Protein-Membrane Interactions: Mechanistic Insight from Model Systems
    • Butterfield, S. M.; Lashuel, H. A. Amyloidogenic Protein-Membrane Interactions: Mechanistic Insight from Model Systems Angew. Chem., Int. Ed. 2010, 49, 2-29
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 2-29
    • Butterfield, S.M.1    Lashuel, H.A.2
  • 25
    • 0037474240 scopus 로고    scopus 로고
    • Metal Ions, pH, and Cholesterol Regulate the Interactions of Alzheimer's Disease Amyloid-β Peptide with Membrane Lipid
    • Curtain, C. C.; Ali, F. E.; Smith, D. G.; Bush, A. I.; Masters, C. L.; Barnham, K. J. Metal Ions, pH, and Cholesterol Regulate the Interactions of Alzheimer's Disease Amyloid-β Peptide with Membrane Lipid J. Biol. Chem. 2003, 278, 2977-2982
    • (2003) J. Biol. Chem. , vol.278 , pp. 2977-2982
    • Curtain, C.C.1    Ali, F.E.2    Smith, D.G.3    Bush, A.I.4    Masters, C.L.5    Barnham, K.J.6
  • 26
    • 79953225854 scopus 로고    scopus 로고
    • 3+ on Amyloid-β Stability, Oligomerization, and Aggregation: Amyloid-β Destabilization Promotes Annular Protofibril Formation
    • 3+ on Amyloid-β Stability, Oligomerization, and Aggregation: Amyloid-β Destabilization Promotes Annular Protofibril Formation J. Biol. Chem. 2011, 286, 9646-9656
    • (2011) J. Biol. Chem. , vol.286 , pp. 9646-9656
    • Chen, W.-T.1    Liao, Y.-H.2    Yu, H.-M.3    Cheng, I.H.4    Chen, Y.-R.5
  • 28
    • 2442461177 scopus 로고    scopus 로고
    • Copper Binding to the Amyloid-β (Aβ) Peptide Associated with Alzheimer's Disease
    • Syme, C. D.; Nadal, R. C.; Rigby, S. E. J.; Viles, J. H. Copper Binding to the Amyloid-β (Aβ) Peptide Associated with Alzheimer's Disease J. Biol. Chem. 2004, 279, 18169-18177
    • (2004) J. Biol. Chem. , vol.279 , pp. 18169-18177
    • Syme, C.D.1    Nadal, R.C.2    Rigby, S.E.J.3    Viles, J.H.4
  • 29
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of Copper Interactions with Alzheimer Amyloid β Peptides: Identification of an Attomolar-Affinity Copper Binding Site on Amyloid β1-42
    • Atwood, C. S.; Scarpa, R. C.; Huang, X.; Moir, R. D.; Jones, W. D.; Fairlie, D. P.; Tanzi, R. E.; Bush, A. I. Characterization of Copper Interactions with Alzheimer Amyloid β Peptides: Identification of an Attomolar-Affinity Copper Binding Site on Amyloid β1-42 J. Neurochem. 2000, 75, 1219-1233
    • (2000) J. Neurochem. , vol.75 , pp. 1219-1233
    • Atwood, C.S.1    Scarpa, R.C.2    Huang, X.3    Moir, R.D.4    Jones, W.D.5    Fairlie, D.P.6    Tanzi, R.E.7    Bush, A.I.8
  • 30
    • 39749137469 scopus 로고    scopus 로고
    • Binding of Zinc(II) and Copper(II) to the Full-Length Alzheimer's Amyloid-β Peptide
    • Tougu, V.; Karafin, A.; Palumaa, P. Binding of Zinc(II) and Copper(II) to the Full-Length Alzheimer's Amyloid-β Peptide J. Neurochem. 2008, 104, 1249-1259
    • (2008) J. Neurochem. , vol.104 , pp. 1249-1259
    • Tougu, V.1    Karafin, A.2    Palumaa, P.3
  • 31
    • 84862525394 scopus 로고    scopus 로고
    • Calorimetric investigation of copper (II) binding to Aβ peptides: Thermodynamics of coordination plasticity.
    • Sacco, C.; Skowronsky, R. A.; Gade, S.; Kenney, J. M.; Spuches, A. M. Calorimetric investigation of copper (II) binding to Aβ peptides: thermodynamics of coordination plasticity. J. Biol. Inorg. Chem. 2012, 17, 531-541
    • (2012) J. Biol. Inorg. Chem. , vol.17 , pp. 531-541
    • Sacco, C.1    Skowronsky, R.A.2    Gade, S.3    Kenney, J.M.4    Spuches, A.M.5
  • 32
    • 48949116132 scopus 로고    scopus 로고
    • Single-Molecule Investigation of the Interactions between Reconstituted Planar Lipid Membranes and an Analogue of the HP(2-20) Antimicrobial Peptide
    • Mereuta, L.; Luchian, T.; Park, Y.; Hahm, K. S. Single-Molecule Investigation of the Interactions between Reconstituted Planar Lipid Membranes and an Analogue of the HP(2-20) Antimicrobial Peptide Biochem. Biophys. Res. Commun. 2008, 373, 467-472
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 467-472
    • Mereuta, L.1    Luchian, T.2    Park, Y.3    Hahm, K.S.4
  • 33
    • 34848857573 scopus 로고    scopus 로고
    • PH Modulation of Transport Properties of Alamethicin Oligomers Inserted in Zwitterionic-Based Artificial Lipid Membranes
    • Chiriac, R.; Luchian, T. pH Modulation of Transport Properties of Alamethicin Oligomers Inserted in Zwitterionic-Based Artificial Lipid Membranes Biophys. Chem. 2007, 130, 139-147
    • (2007) Biophys. Chem. , vol.130 , pp. 139-147
    • Chiriac, R.1    Luchian, T.2
  • 34
    • 78149402689 scopus 로고    scopus 로고
    • DNA Capture into a Nanopore: Interplay of Diffusion and Electrohydrodynamics
    • Grosberg, A. Y.; Rabin, Y. DNA Capture into a Nanopore: Interplay of Diffusion and Electrohydrodynamics J. Chem. Phys. 2010, 133, 165102
    • (2010) J. Chem. Phys. , vol.133 , pp. 165102
    • Grosberg, A.Y.1    Rabin, Y.2
  • 35
    • 76649116514 scopus 로고    scopus 로고
    • Electrostatic Focusing of Unlabeled DNA into Nanoscale Pores using a Salt Gradient
    • Wanunu, M.; Morrison, W.; Rabin, Y.; Grosberg, A. Y.; Meller, A. Electrostatic Focusing of Unlabeled DNA into Nanoscale Pores using a Salt Gradient Nat. Nanotechnol. 2010, 5, 160-165
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 160-165
    • Wanunu, M.1    Morrison, W.2    Rabin, Y.3    Grosberg, A.Y.4    Meller, A.5
  • 36
    • 84866929293 scopus 로고    scopus 로고
    • Studies on the Interactions of Copper and Zinc Ions with β-Amyloid Peptides by a Surface Plasmon Resonance Biosensor
    • Yao, F.; Zhang, R.; Tian, H.; Li, X. Studies on the Interactions of Copper and Zinc Ions with β-Amyloid Peptides by a Surface Plasmon Resonance Biosensor Int. J. Mol. Sci. 2012, 13, 11832-11843
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 11832-11843
    • Yao, F.1    Zhang, R.2    Tian, H.3    Li, X.4
  • 37
    • 49149093778 scopus 로고    scopus 로고
    • Quantification of the Binding Constant of Copper(II) to the Amyloid-β Peptide
    • Hatcher, L. Q.; Hong, L.; Bush, W. D.; Carducci, T.; Simon, J. Quantification of the Binding Constant of Copper(II) to the Amyloid-β Peptide J. Phys. Chem. B 2008, 112, 8160-8164
    • (2008) J. Phys. Chem. B , vol.112 , pp. 8160-8164
    • Hatcher, L.Q.1    Hong, L.2    Bush, W.D.3    Carducci, T.4    Simon, J.5
  • 38
    • 81855183533 scopus 로고    scopus 로고
    • Copper(II) Interaction with Amyloid-β: Affinity and Speciation
    • Arena, G.; Pappalardo, G.; Sovago, I.; Rizzarelli, E. Copper(II) Interaction with Amyloid-β: Affinity and Speciation Coord. Chem. Rev. 2012, 256, 3-12
    • (2012) Coord. Chem. Rev. , vol.256 , pp. 3-12
    • Arena, G.1    Pappalardo, G.2    Sovago, I.3    Rizzarelli, E.4
  • 41
    • 33845665797 scopus 로고    scopus 로고
    • High-Resolution NMR Studies of the Zinc-Binding Site of the Alzheimer's Amyloid β-Peptide
    • Danielsson, J.; Pierattelli, R.; Banci, L.; Graslund, A. High-Resolution NMR Studies of the Zinc-Binding Site of the Alzheimer's Amyloid β-Peptide FEBS J. 2007, 274, 46-59
    • (2007) FEBS J. , vol.274 , pp. 46-59
    • Danielsson, J.1    Pierattelli, R.2    Banci, L.3    Graslund, A.4
  • 42
    • 33746590221 scopus 로고    scopus 로고
    • Transport of α-Helical Peptides through α-Hemolysin and Aerolysin Pores
    • Stefureac, R.; Long, Y.-T.; Kraatz, H.-B.; Howard, P.; Lee, J. S. Transport of α-Helical Peptides through α-Hemolysin and Aerolysin Pores Biochemistry 2006, 45, 9172-9179
    • (2006) Biochemistry , vol.45 , pp. 9172
    • Stefureac, R.1    Long, Y.-T.2    Kraatz, H.-B.3    Howard, P.4    Lee, J.S.5


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