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Volumn 29, Issue 46, 2013, Pages 14239-14245

Omega-3 fatty acids regulate the interaction of the Alzheimer's Aβ(25-35) peptide with lipid membranes

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S DISEASE; BIOPHYSICAL PROPERTIES; DYNAMICAL PROPERTIES; LIPID ACYL-CHAINS; MOLECULAR MECHANISM; NEURONAL MEMBRANES; OMEGA-3-FATTY ACIDS; SELF AGGREGATION;

EID: 84888359848     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la403416b     Document Type: Article
Times cited : (37)

References (42)
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics
    • Hardy, J. L.; Selkoe, D. J. The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics Science 2002, 297, 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.L.1    Selkoe, D.J.2
  • 3
    • 84869887960 scopus 로고    scopus 로고
    • Structural Features and Cytotoxicity of Amyloid Oligomers: Implications in Alzheimer's Disease and Other Diseases with Amyloid Deposits
    • Stefani, M. Structural Features and Cytotoxicity of Amyloid Oligomers: Implications in Alzheimer's Disease and Other Diseases with Amyloid Deposits Prog. Neurobiol. 2012, 99, 226-245
    • (2012) Prog. Neurobiol. , vol.99 , pp. 226-245
    • Stefani, M.1
  • 4
    • 84863986886 scopus 로고    scopus 로고
    • Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity
    • Fändrich, M. Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity J. Mol. Biol. 2012, 421, 427-440
    • (2012) J. Mol. Biol. , vol.421 , pp. 427-440
    • Fändrich, M.1
  • 6
    • 84870035190 scopus 로고    scopus 로고
    • Dietary Polyphenol-Derived Protection Against Neurotoxic β-Amyloid Protein: From Molecular to Clinical
    • Smid, S. D.; Maaga, J. L.; Musgrave, I. F. Dietary Polyphenol-Derived Protection Against Neurotoxic β-Amyloid Protein: From Molecular to Clinical Food Funct. 2012, 3, 1242-1250
    • (2012) Food Funct. , vol.3 , pp. 1242-1250
    • Smid, S.D.1    Maaga, J.L.2    Musgrave, I.F.3
  • 7
    • 84880701874 scopus 로고    scopus 로고
    • Current Evidence for the Clinical Use of Long-Chain Polyunsaturated N-3 Fatty Acids to Prevent Age-Related Cognitive Decline and Alzheimer's Disease
    • Dacks, P. A.; Shineman, D. W.; Fillit, H. M. Current Evidence for the Clinical Use of Long-Chain Polyunsaturated N-3 Fatty Acids to Prevent Age-Related Cognitive Decline and Alzheimer's Disease J. Nutr., Health Aging 2013, 17, 240-251
    • (2013) J. Nutr., Health Aging , vol.17 , pp. 240-251
    • Dacks, P.A.1    Shineman, D.W.2    Fillit, H.M.3
  • 8
    • 0025913434 scopus 로고
    • Fatty Acid Composition of Brain Phospholipids in Aging and in Alzheimer's Disease
    • Soderberg, M.; Edlund, C.; Kristensson, K.; Dallner, G. Fatty Acid Composition of Brain Phospholipids in Aging and in Alzheimer's Disease Lipids 1991, 26, 421-425
    • (1991) Lipids , vol.26 , pp. 421-425
    • Soderberg, M.1    Edlund, C.2    Kristensson, K.3    Dallner, G.4
  • 9
    • 84855759607 scopus 로고    scopus 로고
    • The Effects of Long-Term Omega-3 Fatty Acid Supplementation on Cognition and Alzheimer's Pathology in Animal Models of Alzheimer's Disease: A Systematic Review and Meta-Analysis
    • Hooijmans, C. R.; Pasker-de Jong, P. C. M.; de Vries, R. B. M.; Ritskes-Hoitinga, M. The Effects of Long-Term Omega-3 Fatty Acid Supplementation on Cognition and Alzheimer's Pathology in Animal Models of Alzheimer's Disease: A Systematic Review and Meta-Analysis J. Alzheimer's Dis. 2012, 28, 191-209
    • (2012) J. Alzheimer's Dis. , vol.28 , pp. 191-209
    • Hooijmans, C.R.1    Pasker-De Jong, P.C.M.2    De Vries, R.B.M.3    Ritskes-Hoitinga, M.4
  • 11
    • 57049137646 scopus 로고    scopus 로고
    • Experimental Models and Mechanisms Underlying the Protective Effects of n-3 Polyunsaturated Fatty Acids in Alzheimer's Disease
    • Boudreault, C.; Bazinet, R. P.; Ma, D. W. Experimental Models and Mechanisms Underlying the Protective Effects of n-3 Polyunsaturated Fatty Acids in Alzheimer's Disease J. Nutr. Biochem. 2009, 20, 1-10
    • (2009) J. Nutr. Biochem. , vol.20 , pp. 1-10
    • Boudreault, C.1    Bazinet, R.P.2    Ma, D.W.3
  • 13
    • 77951173605 scopus 로고    scopus 로고
    • Omega-3 Fatty Acids: Potential Role in the Management of Early Alzheimer's Disease
    • Jicha, G. A.; Markesbery, W. R. Omega-3 Fatty Acids: Potential Role in the Management of Early Alzheimer's Disease Journal of Clinical Interventions in Aging 2010, 5, 45-61
    • (2010) Journal of Clinical Interventions in Aging , vol.5 , pp. 45-61
    • Jicha, G.A.1    Markesbery, W.R.2
  • 15
    • 80053589341 scopus 로고    scopus 로고
    • Membrane and Surface Interactions of Alzheimer's Aβ Peptide: Insights into the Mechanism of Cytotoxicity
    • Williams, T. L.; Serpell, L. C. Membrane and Surface Interactions of Alzheimer's Aβ Peptide: Insights into the Mechanism of Cytotoxicity FEBS J. 2011, 278, 3905-3917
    • (2011) FEBS J. , vol.278 , pp. 3905-3917
    • Williams, T.L.1    Serpell, L.C.2
  • 16
    • 0028981219 scopus 로고
    • Structure-Activity Analyses of β-Amyloid Peptides: Contributions of the Aβ25-35 Region to Aggregation and Neurotoxicity
    • Pike, C. J.; Walencewicz-Wasserman, A. J.; Kosmoski, J.; Cribbs, D. H.; Glabe, C. G.; Cotman, C. W. Structure-Activity Analyses of β-Amyloid Peptides: Contributions of the Aβ25-35 Region to Aggregation and Neurotoxicity J. Neurochem. 1995, 64, 253-265
    • (1995) J. Neurochem. , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 17
    • 36849095507 scopus 로고    scopus 로고
    • Cholesterol and Clioquinol Modulation of Aβ(1-42) Interaction with Phospholipid Bilayers and Metals
    • Lau, T.-L.; Gehman, J. D.; Wade, J. D.; Masters, C. L.; Barnham, K. J.; Separovic, F. Cholesterol and Clioquinol Modulation of Aβ(1-42) Interaction with Phospholipid Bilayers and Metals Biochim. Biophys. Acta 2007, 1768, 3135-3144
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3135-3144
    • Lau, T.-L.1    Gehman, J.D.2    Wade, J.D.3    Masters, C.L.4    Barnham, K.J.5    Separovic, F.6
  • 18
    • 34948814069 scopus 로고    scopus 로고
    • Membrane Interactions and the Effect of Metal Ions of the Amyloidogenic Fragment Aβ(25-35) in Comparison to Aβ(1-42)
    • Lau, T. L.; Gehman, J. D.; Wade, J. D.; Perez, K.; Masters, C. L.; Barnham, K. J.; Separovic, F. Membrane Interactions and the Effect of Metal Ions of the Amyloidogenic Fragment Aβ(25-35) in Comparison to Aβ(1-42) Biochim. Biophys. Acta 2007, 1768, 2400-2408
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2400-2408
    • Lau, T.L.1    Gehman, J.D.2    Wade, J.D.3    Perez, K.4    Masters, C.L.5    Barnham, K.J.6    Separovic, F.7
  • 19
    • 34249051698 scopus 로고    scopus 로고
    • Amide Solvent Protection Analysis Demonstrates That Amyloid-β(1-40) and Amyloid-β(1-42) Form Different Fibrillar Structures under Identical Conditions
    • Olofsson, A.; Lindhagen-Persson, M.; Sauer-Eriksson, A. E.; Ohman, A. Amide Solvent Protection Analysis Demonstrates That Amyloid-β(1-40) and Amyloid-β(1-42) Form Different Fibrillar Structures under Identical Conditions Biochem. J. 2007, 404, 63-70
    • (2007) Biochem. J. , vol.404 , pp. 63-70
    • Olofsson, A.1    Lindhagen-Persson, M.2    Sauer-Eriksson, A.E.3    Ohman, A.4
  • 21
    • 84869855723 scopus 로고    scopus 로고
    • Amyloid β-Peptide 25-35 Self-Assembly and Its Inhibition: A Model Undecapeptide System to Gain Atomistic and Secondary Structure Details of the Alzheimer's Disease Process and Treatment
    • Naldi, M.; Fiori, J.; Pistolozzi, M.; Drake, A. F.; Bertucci, C.; Wu, R.; Mlynarczyk, K.; Filipek, S.; De Simone, A.; Andrisano, V. Amyloid β-Peptide 25-35 Self-Assembly and Its Inhibition: A Model Undecapeptide System to Gain Atomistic and Secondary Structure Details of the Alzheimer's Disease Process and Treatment ACS Chem. Neurosci. 2012, 3, 952-962
    • (2012) ACS Chem. Neurosci. , vol.3 , pp. 952-962
    • Naldi, M.1    Fiori, J.2    Pistolozzi, M.3    Drake, A.F.4    Bertucci, C.5    Wu, R.6    Mlynarczyk, K.7    Filipek, S.8    De Simone, A.9    Andrisano, V.10
  • 22
    • 0028873175 scopus 로고
    • Lipid Composition of Neuronal Cell Bodies and Neurites from Cultured Dorsal Root Ganglia
    • Calderon, R. O.; Attema, B.; DeVrie, G. H. Lipid Composition of Neuronal Cell Bodies and Neurites from Cultured Dorsal Root Ganglia J. Neurochem. 1995, 64, 424-429
    • (1995) J. Neurochem. , vol.64 , pp. 424-429
    • Calderon, R.O.1    Attema, B.2    Devrie, G.H.3
  • 23
    • 79954489046 scopus 로고    scopus 로고
    • Neuronal Membranes are Key to the Pathogenesis of Alzheimer's Disease: The Role of Both Raft and Non-Raft Membrane Domains
    • Williamson, R.; Sutherland, C. Neuronal Membranes are Key to the Pathogenesis of Alzheimer's Disease: The Role of Both Raft and Non-Raft Membrane Domains Curr. Alzheimer Res. 2011, 8, 213-221
    • (2011) Curr. Alzheimer Res. , vol.8 , pp. 213-221
    • Williamson, R.1    Sutherland, C.2
  • 24
    • 55749114033 scopus 로고    scopus 로고
    • Interaction Between Alzheimer's Aβ(25-35) Peptide and Phospholipid Bilayers: The Role of Cholesterol
    • D'Errico, G.; Vitiello, G.; Ortona, O.; Tedeschi, A.; Ramunno, A.; D'Ursi, A. M. Interaction Between Alzheimer's Aβ(25-35) Peptide and Phospholipid Bilayers: The Role of Cholesterol Biochim. Biophys. Acta 2008, 1778, 2710-2716
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2710-2716
    • D'errico, G.1    Vitiello, G.2    Ortona, O.3    Tedeschi, A.4    Ramunno, A.5    D'ursi, A.M.6
  • 25
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an Online Server for Protein Secondary Structure Analyses from Circular Dichroism Spectroscopic Data
    • Whitmore, L.; Wallace, B. DICHROWEB, an Online Server for Protein Secondary Structure Analyses from Circular Dichroism Spectroscopic Data Nucleic Acids Res. 2004, 32, W668-W673
    • (2004) Nucleic Acids Res. , vol.32
    • Whitmore, L.1    Wallace, B.2
  • 28
    • 45449105164 scopus 로고    scopus 로고
    • Protein Modulation of Lipids and Vice Versa in Membranes
    • Marsh, D. Protein Modulation of Lipids and Vice Versa in Membranes Biochim. Biophys. Acta 2008, 1778, 1545-1575
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1545-1575
    • Marsh, D.1
  • 29
    • 80054769975 scopus 로고    scopus 로고
    • Enforcing the Positive Charge of N-Termini Enhances Membrane Interaction and Antitumor Activity of Bovine Seminal Ribonuclease
    • D'Errico, G.; Ercole, C.; Lista, M.; Pizzo, E.; Falanga, A.; Galdiero, S.; Spadaccini, R.; Picone, D. Enforcing the Positive Charge of N-Termini Enhances Membrane Interaction and Antitumor Activity of Bovine Seminal Ribonuclease Biochim. Biophys. Acta 2011, 1808, 3007-3015
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 3007-3015
    • D'errico, G.1    Ercole, C.2    Lista, M.3    Pizzo, E.4    Falanga, A.5    Galdiero, S.6    Spadaccini, R.7    Picone, D.8
  • 30
    • 0002144978 scopus 로고
    • Electron Spin Resonance Analysis of Model and Biological Membranes
    • In; Aloia, R. C. Curtain, C. C. Gordon, L. M. Alan R. Liss: New York - 89
    • Gordon, L. M.; Curtain, C. C. Electron Spin Resonance Analysis of Model and Biological Membranes. In Advances in Membrane Fluidity 1: Methods for Studying Membrane Fluidity; Aloia, R. C.; Curtain, C. C.; Gordon, L. M., Eds.; Alan R. Liss: New York, 1988, pp 25-89.
    • (1988) Advances in Membrane Fluidity 1: Methods for Studying Membrane Fluidity , pp. 25
    • Gordon, L.M.1    Curtain, C.C.2
  • 33
    • 0037133849 scopus 로고    scopus 로고
    • Interactions between Starburst Dendrimers and Mixed DMPC/DMPA-Na Vesicles Studied by the Spin Label and the Spin Probe Techniques, Supported by TEM
    • Ottaviani, M. F.; Favuzza, P.; Sacchi, B.; Turro, N. J.; Jockusch, S.; Tomalia, D. A. Interactions between Starburst Dendrimers and Mixed DMPC/DMPA-Na Vesicles Studied by the Spin Label and the Spin Probe Techniques, Supported by TEM Langmuir 2002, 18, 2347-2357
    • (2002) Langmuir , vol.18 , pp. 2347-2357
    • Ottaviani, M.F.1    Favuzza, P.2    Sacchi, B.3    Turro, N.J.4    Jockusch, S.5    Tomalia, D.A.6
  • 34
  • 35
    • 77649153302 scopus 로고    scopus 로고
    • Sponge Mesoporous Silica Formation Using Disordered Phospholipid Bilayers as Template
    • Di Renzo, F.; Ottaviani, M. F. Sponge Mesoporous Silica Formation Using Disordered Phospholipid Bilayers as Template J. Phys. Chem. B 2010, 114, 2140-2152
    • (2010) J. Phys. Chem. B , vol.114 , pp. 2140-2152
    • Di Renzo, F.1    Ottaviani, M.F.2
  • 36
    • 84883485263 scopus 로고    scopus 로고
    • Effect of Hydrogenated Cardanol on the Structure of Model Membranes Studied by EPR and NMR
    • Santeusanio, S.; Attanasi, O. A.; Majer, R.; Cangiotti, M.; Fattori, A.; Ottaviani, M. F. Effect of Hydrogenated Cardanol on the Structure of Model Membranes Studied by EPR and NMR Langmuir 2013, 29, 11118-11126
    • (2013) Langmuir , vol.29 , pp. 11118-11126
    • Santeusanio, S.1    Attanasi, O.A.2    Majer, R.3    Cangiotti, M.4    Fattori, A.5    Ottaviani, M.F.6
  • 37
    • 84879232509 scopus 로고    scopus 로고
    • On the Mechanism of Ion Transport through Lipid Membranes Mediated By PEGylated Cyclic Oligosaccharides (CyPLOS): An ESR Study
    • Busi, E.; Vitiello, G.; Niccoli, M.; Basosi, R.; Montesarchio, D.; D'Errico, G. On the Mechanism of Ion Transport through Lipid Membranes Mediated By PEGylated Cyclic Oligosaccharides (CyPLOS): An ESR Study Biochim. Biophys. Acta 2013, 1828, 2074-2082
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 2074-2082
    • Busi, E.1    Vitiello, G.2    Niccoli, M.3    Basosi, R.4    Montesarchio, D.5    D'errico, G.6
  • 38
    • 76749161946 scopus 로고    scopus 로고
    • Liquid-Ordered Phases Induced by Cholesterol: A Compendium of Binary Phase Diagrams
    • Marsh, D. Liquid-Ordered Phases Induced by Cholesterol: A Compendium of Binary Phase Diagrams Biochim. Biophys. Acta 2010, 1798, 688-699
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 688-699
    • Marsh, D.1
  • 39
    • 84855759411 scopus 로고    scopus 로고
    • The iAβ5p β-Breaker Peptide Regulates the Aβ(25-35) Interaction with Lipid Bilayers Through a Cholesterol-Mediated Mechanism
    • Vitiello, G.; Grimaldi, M.; D'Ursi, A. M.; D'Errico, G. The iAβ5p β-Breaker Peptide Regulates the Aβ(25-35) Interaction with Lipid Bilayers Through a Cholesterol-Mediated Mechanism Biochem. Biophys. Res. Commun. 2012, 417, 88-92
    • (2012) Biochem. Biophys. Res. Commun. , vol.417 , pp. 88-92
    • Vitiello, G.1    Grimaldi, M.2    D'ursi, A.M.3    D'errico, G.4
  • 40
    • 70349481144 scopus 로고    scopus 로고
    • Cholesterol-Induced Fluid Membrane Domains: A Compendium of Lipid-Raft Ternary Phase Diagrams
    • Marsh, D. Cholesterol-Induced Fluid Membrane Domains: A Compendium of Lipid-Raft Ternary Phase Diagrams Biochim. Biophys. Acta 2009, 1788, 2114-2123
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2114-2123
    • Marsh, D.1
  • 42
    • 77955060978 scopus 로고    scopus 로고
    • Membrane Biophysics and Mechanics in Alzheimer's Disease
    • Yang, X.; Askarova, S.; Lee, J. C. Membrane Biophysics and Mechanics in Alzheimer's Disease Mol. Neurobiol. 2010, 41, 138-148
    • (2010) Mol. Neurobiol. , vol.41 , pp. 138-148
    • Yang, X.1    Askarova, S.2    Lee, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.