메뉴 건너뛰기




Volumn 417, Issue 1, 2012, Pages 88-92

The iAβ5p β-breaker peptide regulates the Aβ(25-35) interaction with lipid bilayers through a cholesterol-mediated mechanism

Author keywords

Amyloid; Sheet breaker; Cholesterol; Electron Spin Resonance; Lipid bilayer

Indexed keywords

AMYLOID BETA PROTEIN[25-35]; CHOLESTEROL; IABETA5P PROTEIN; PHOSPHOLIPID; PROTEIN; UNCLASSIFIED DRUG;

EID: 84855759411     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.11.061     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 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
  • 2
    • 0033597105 scopus 로고    scopus 로고
    • γ-Secretase, evidence for multiple proteolytic activities and influence of membrane positioning of substrate on generation of amyloid β peptides of varying length
    • Murphy M.P., Hickman L.J., Eckman C.B., Uljon S.N., Wang R., Golde T.E. γ-Secretase, evidence for multiple proteolytic activities and influence of membrane positioning of substrate on generation of amyloid β peptides of varying length. J. Biol. Chem. 1999, 274:11914-11923.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11914-11923
    • Murphy, M.P.1    Hickman, L.J.2    Eckman, C.B.3    Uljon, S.N.4    Wang, R.5    Golde, T.E.6
  • 3
    • 24144437434 scopus 로고    scopus 로고
    • A rapid label-free electrochemical detection and kinetic study of Alzheimer's amyloid β aggregation
    • Vestergaard M., Kerman K., Masato S., Nagatani N., Takamura Y., Tamiya E. A rapid label-free electrochemical detection and kinetic study of Alzheimer's amyloid β aggregation. J. Am. Chem. Soc. 2005, 127:11892-11893.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11892-11893
    • Vestergaard, M.1    Kerman, K.2    Masato, S.3    Nagatani, N.4    Takamura, Y.5    Tamiya, E.6
  • 4
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state
    • Pike C.J., Burdick D., Walencewicz A.J., Glabe C.G., Cotman C.W. Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 1993, 13:1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 5
    • 0031170886 scopus 로고    scopus 로고
    • The toxicity of the Alzheimer's β-amyloid peptide correlates with a distinct fiber morphology
    • Seilheimer B., Bohrmann B., Bondolfi L., Muller F., Stuber D., Dobeli H. The toxicity of the Alzheimer's β-amyloid peptide correlates with a distinct fiber morphology. J. Struct. Biol. 1997, 119:59-71.
    • (1997) J. Struct. Biol. , vol.119 , pp. 59-71
    • Seilheimer, B.1    Bohrmann, B.2    Bondolfi, L.3    Muller, F.4    Stuber, D.5    Dobeli, H.6
  • 6
    • 33645830313 scopus 로고    scopus 로고
    • Vicious cycles within the neuropathophysiologic mechanisms of Alzheimer's disease
    • Standridge J.B. Vicious cycles within the neuropathophysiologic mechanisms of Alzheimer's disease. Curr. Alzheimer Res. 2006, 3:95-108.
    • (2006) Curr. Alzheimer Res. , vol.3 , pp. 95-108
    • Standridge, J.B.1
  • 7
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA type glutamate receptor-dependent signaling pathway
    • Shankar G.M., Bloodgood B.L., Townsend M., Walsh D.M., Selkoe D.J., Sabatini B.L. Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA type glutamate receptor-dependent signaling pathway. J. Neurosci. 2007, 27:2866-2875.
    • (2007) J. Neurosci. , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 9
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation
    • Soto C., Kindy M.S., Baumann M., Frangione B. Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation. Biochem. Biophys. Res. Commun. 1996, 226:672-680.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 672-680
    • Soto, C.1    Kindy, M.S.2    Baumann, M.3    Frangione, B.4
  • 10
    • 0031873102 scopus 로고    scopus 로고
    • β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy
    • Soto C., Sigurdsson E.M., Morelli L., Kumar R.A., Castaño E.M., Frangione B. β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nat. Med. 1998, 4:822-826.
    • (1998) Nat. Med. , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castaño, E.M.5    Frangione, B.6
  • 11
    • 0032839878 scopus 로고    scopus 로고
    • Plaque busters: strategies to inhibit amyloid formation in Alzheimer's disease
    • Soto C. Plaque busters: strategies to inhibit amyloid formation in Alzheimer's disease. Mol. Med. Today 1999, 5:343-350.
    • (1999) Mol. Med. Today , vol.5 , pp. 343-350
    • Soto, C.1
  • 12
    • 0036597960 scopus 로고    scopus 로고
    • Beta-sheet breaker strategy for the treatment of Alzheimer's disease
    • Adessi C., Soto C. Beta-sheet breaker strategy for the treatment of Alzheimer's disease. Drug Dev. Res. 2002, 56:184-193.
    • (2002) Drug Dev. Res. , vol.56 , pp. 184-193
    • Adessi, C.1    Soto, C.2
  • 14
    • 34547350809 scopus 로고    scopus 로고
    • Physicochemical interactions of amyloid β-peptide with lipid bilayers
    • Matsuzaki K. Physicochemical interactions of amyloid β-peptide with lipid bilayers. Biochim. Biophys. Acta 2007, 1768:1935-1942.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1935-1942
    • Matsuzaki, K.1
  • 15
    • 33646557678 scopus 로고    scopus 로고
    • The role of lipid-protein interactions in amyloid-type protein fibril formation
    • Gorbenko G.P., Kinnunen P.K. The role of lipid-protein interactions in amyloid-type protein fibril formation. Chem. Phys. Lipids 2006, 141:72-82.
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 72-82
    • Gorbenko, G.P.1    Kinnunen, P.K.2
  • 17
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: contributions of the β 25-35 region to aggregation and neuro toxicity
    • 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 β 25-35 region to aggregation and neuro toxicity. 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
  • 18
    • 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
  • 19
    • 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
  • 20
    • 0002316753 scopus 로고
    • Spin-labeling and lipid-protein interactions in membranes
    • Wiley Interscience, New York
    • Marsh D., Watts A. Spin-labeling and lipid-protein interactions in membranes. Lipid-Protein Interactions 1982, vol. 2:53-126. Wiley Interscience, New York.
    • (1982) Lipid-Protein Interactions , vol.2 , pp. 53-126
    • Marsh, D.1    Watts, A.2
  • 21
    • 55649110254 scopus 로고    scopus 로고
    • Electron spin resonance in membrane research: protein-lipid interactions
    • Marsh D. Electron spin resonance in membrane research: protein-lipid interactions. Methods 2008, 46:83-96.
    • (2008) Methods , vol.46 , pp. 83-96
    • Marsh, D.1
  • 22
    • 0026743982 scopus 로고
    • The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: peptide conformation, orientation and aggregation
    • Gordon L.M., Curtain C.C., Zhong Y.C., Kirkpatrick A., Mobley P.W., Waring A.J. The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: peptide conformation, orientation and aggregation. Biochim. Biophys. Acta 1992, 1139:257-274.
    • (1992) Biochim. Biophys. Acta , vol.1139 , pp. 257-274
    • Gordon, L.M.1    Curtain, C.C.2    Zhong, Y.C.3    Kirkpatrick, A.4    Mobley, P.W.5    Waring, A.J.6
  • 23
    • 0033024286 scopus 로고    scopus 로고
    • The interactions of the N-terminal fusogenic peptide of HIV-1 gp41 with neutral phospholipids
    • Curtain C., Separovic F., Nielsen K., Craik D., Zhong Y., Kirkpatrick A. The interactions of the N-terminal fusogenic peptide of HIV-1 gp41 with neutral phospholipids. Eur. Biophys. J. 1999, 28:427-436.
    • (1999) Eur. Biophys. J. , vol.28 , pp. 427-436
    • Curtain, C.1    Separovic, F.2    Nielsen, K.3    Craik, D.4    Zhong, Y.5    Kirkpatrick, A.6
  • 25
    • 43249131758 scopus 로고    scopus 로고
    • Interaction of a peptide derived from glycoprotein gp36 of feline immunodeficiency virus and its lipoylated analogue with phospholipid membranes
    • D'Errico G., D'Ursi A.M., Marsh D. Interaction of a peptide derived from glycoprotein gp36 of feline immunodeficiency virus and its lipoylated analogue with phospholipid membranes. Biochemistry 2008, 47:5317-5327.
    • (2008) Biochemistry , vol.47 , pp. 5317-5327
    • D'Errico, G.1    D'Ursi, A.M.2    Marsh, D.3
  • 26
    • 69049108658 scopus 로고    scopus 로고
    • Interaction of short modified peptides deriving from glycoprotein gp36 of feline immunodeficiency virus with phospholipid membranes
    • D'Errico G., Vitiello G., D'Ursi A.M., Marsh D. Interaction of short modified peptides deriving from glycoprotein gp36 of feline immunodeficiency virus with phospholipid membranes. Eur. Biophys. J. 2009, 38:873-882.
    • (2009) Eur. Biophys. J. , vol.38 , pp. 873-882
    • D'Errico, G.1    Vitiello, G.2    D'Ursi, A.M.3    Marsh, D.4
  • 27
    • 79961102115 scopus 로고    scopus 로고
    • Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes
    • Vitiello G., Falanga A., Galdiero M., Marsh D., Galdiero S., D'Errico G. Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes. Biochim. Biophys. Acta 2011, 1808:2517-2526.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2517-2526
    • Vitiello, G.1    Falanga, A.2    Galdiero, M.3    Marsh, D.4    Galdiero, S.5    D'Errico, G.6
  • 28
    • 0344589334 scopus 로고    scopus 로고
    • Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin labelling
    • Marsh D., Horvath L.I. Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin labelling. Biochim. Biophys. Acta 1998, 1376:267-296.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 267-296
    • Marsh, D.1    Horvath, L.I.2
  • 29
    • 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
  • 30
    • 58849083755 scopus 로고    scopus 로고
    • Phase equilibria in DOPC/DPPC-d62/cholesterol mixtures
    • Davis J.H., Clair J.J., Juhasz J. Phase equilibria in DOPC/DPPC-d62/cholesterol mixtures. Biophys. J. 2009, 96:521-539.
    • (2009) Biophys. J. , vol.96 , pp. 521-539
    • Davis, J.H.1    Clair, J.J.2    Juhasz, J.3
  • 31
    • 0015241658 scopus 로고
    • Molecular motion in spin-labelled phospholipids and membranes
    • Hubbell W., McConnell H.M. Molecular motion in spin-labelled phospholipids and membranes. J. Am. Chem. Soc. 1971, 93:314-326.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 314-326
    • Hubbell, W.1    McConnell, H.M.2
  • 32
    • 0017623581 scopus 로고
    • Studies on spin-labelled egg lecithin dispersions
    • Gordon L.M., Sauerheber R.D. Studies on spin-labelled egg lecithin dispersions. Biochim. Biophys. Acta 1977, 466:34-43.
    • (1977) Biochim. Biophys. Acta , vol.466 , pp. 34-43
    • Gordon, L.M.1    Sauerheber, R.D.2
  • 33
    • 0002144978 scopus 로고
    • Electron spin resonance analysis of model and biological membranes
    • Alan R. Liss, New York, R.C. Aloia, C.C. Curtain, L.M. Gordon (Eds.)
    • Gordon L.M., Curtain C.C. Electron spin resonance analysis of model and biological membranes. Advances in Membrane Fluidity 1: Methods for Studying Membrane Fluidity 1988, 25-89. Alan R. Liss, New York. R.C. Aloia, C.C. Curtain, L.M. Gordon (Eds.).
    • (1988) Advances in Membrane Fluidity 1: Methods for Studying Membrane Fluidity , pp. 25-89
    • Gordon, L.M.1    Curtain, C.C.2
  • 36
    • 0041530267 scopus 로고    scopus 로고
    • Membrane-anchoring and charge effects in the interaction of myelin basic protein with lipid bilayers studied by site-directed spin labelling
    • Bates I.R., Boggs J.M., Feix J.B., Harauz G. Membrane-anchoring and charge effects in the interaction of myelin basic protein with lipid bilayers studied by site-directed spin labelling. J. Biol. Chem. 2003, 278:29041-29047.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29041-29047
    • Bates, I.R.1    Boggs, J.M.2    Feix, J.B.3    Harauz, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.