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Volumn 376, Issue 1, 2008, Pages 56-59

Non-electrostatic binding and self-association of amyloid β-peptide on the surface of tightly packed phosphatidylcholine membranes

Author keywords

Amyloid peptide; Circular dichroism; Lipid phase transition; Peptide secondary structure; Peptide lipid interaction; Phosphatidylcholine; Self association

Indexed keywords

AMYLOID BETA PROTEIN; PHOSPHATIDYLCHOLINE;

EID: 52049116287     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.08.093     Document Type: Article
Times cited : (41)

References (15)
  • 1
    • 0027195933 scopus 로고
    • Seeding one-dimensional crystallization of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett J.T., and Lansbury Jr. P.T. Seeding one-dimensional crystallization of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?. Cell 73 (1993) 1055-1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 2
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid β induce neurotoxicity by distinct mechanisms in human cortical neurons
    • Deshpande A., Mina E., Glabe C., and Busciglio J. Different conformations of amyloid β induce neurotoxicity by distinct mechanisms in human cortical neurons. J. Neurosci. 26 (2006) 6011-6018
    • (2006) J. Neurosci. , vol.26 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 4
    • 0342378042 scopus 로고    scopus 로고
    • Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes
    • Terzi E., Hölzemann G., and Seelig J. Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes. Biochemistry 36 (1997) 14845-14852
    • (1997) Biochemistry , vol.36 , pp. 14845-14852
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 5
    • 0347753786 scopus 로고    scopus 로고
    • Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation
    • Bokvist M., Lindström F., Watts A., and Gröbner G. Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J. Mol. Biol. 335 (2004) 1039-1049
    • (2004) J. Mol. Biol. , vol.335 , pp. 1039-1049
    • Bokvist, M.1    Lindström, F.2    Watts, A.3    Gröbner, G.4
  • 6
    • 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 1768 (2007) 1935-1942
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1935-1942
    • Matsuzaki, K.1
  • 7
    • 0034697010 scopus 로고    scopus 로고
    • Sphingolipid-enriched membrane domains from rat cerebellar granule cells differentiated in culture
    • Prinetti A., Chigorno V., Tettamanti G., and Sonnino S. Sphingolipid-enriched membrane domains from rat cerebellar granule cells differentiated in culture. J. Biol. Chem. 275 (2000) 11658-11665
    • (2000) J. Biol. Chem. , vol.275 , pp. 11658-11665
    • Prinetti, A.1    Chigorno, V.2    Tettamanti, G.3    Sonnino, S.4
  • 8
    • 35348849675 scopus 로고    scopus 로고
    • Clustered negative charges on the lipid membrane surface induce β-sheet formation of prion protein fragment 106-126
    • Miura T., Yoda M., Takaku N., Hirose T., and Takeuchi H. Clustered negative charges on the lipid membrane surface induce β-sheet formation of prion protein fragment 106-126. Biochemistry 46 (2007) 11589-11597
    • (2007) Biochemistry , vol.46 , pp. 11589-11597
    • Miura, T.1    Yoda, M.2    Takaku, N.3    Hirose, T.4    Takeuchi, H.5
  • 9
    • 0032578027 scopus 로고    scopus 로고
    • Phases and phase transitions of the phosphatidylcholines
    • Koynova R., and Caffrey M. Phases and phase transitions of the phosphatidylcholines. Biochim. Biophys. Acta 1376 (1998) 91-145
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 91-145
    • Koynova, R.1    Caffrey, M.2
  • 10
    • 0019005874 scopus 로고
    • Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
    • Brahms S., and Brahms J. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138 (1980) 149-178
    • (1980) J. Mol. Biol. , vol.138 , pp. 149-178
    • Brahms, S.1    Brahms, J.2
  • 11
    • 16644384871 scopus 로고    scopus 로고
    • Structural calorimetry of main transition of supported DMPC bilayers by temperature-controlled AFM
    • Enders O., Ngezahayo A., Wiechmann M., Leisten F., and Kolb H.-A. Structural calorimetry of main transition of supported DMPC bilayers by temperature-controlled AFM. Biophys. J. 87 (2004) 2522-2531
    • (2004) Biophys. J. , vol.87 , pp. 2522-2531
    • Enders, O.1    Ngezahayo, A.2    Wiechmann, M.3    Leisten, F.4    Kolb, H.-A.5
  • 12
    • 0032740652 scopus 로고    scopus 로고
    • Calorimetric and molecular mechanics studies of the thermotropic phase behavior of membrane phospholipids
    • Huang C., and Li S. Calorimetric and molecular mechanics studies of the thermotropic phase behavior of membrane phospholipids. Biochim. Biophys. Acta 1422 (1999) 273-307
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 273-307
    • Huang, C.1    Li, S.2
  • 13
    • 0022407355 scopus 로고
    • Cross polarization P-31 nuclear magnetic resonance of phospholipids
    • Frye J., Albert A.D., Selinsky B.S., and Yeagle P.L. Cross polarization P-31 nuclear magnetic resonance of phospholipids. Biophys. J. 48 (1985) 547-552
    • (1985) Biophys. J. , vol.48 , pp. 547-552
    • Frye, J.1    Albert, A.D.2    Selinsky, B.S.3    Yeagle, P.L.4
  • 14
    • 0242385390 scopus 로고    scopus 로고
    • Molecular simulation study of phospholipid bilayers and insights of the interactions with disaccharides
    • Sum A.K., Faller R., and de Pablo J.J. Molecular simulation study of phospholipid bilayers and insights of the interactions with disaccharides. Biophys. J. 85 (2003) 2830-2844
    • (2003) Biophys. J. , vol.85 , pp. 2830-2844
    • Sum, A.K.1    Faller, R.2    de Pablo, J.J.3
  • 15
    • 33845406090 scopus 로고    scopus 로고
    • Preferential accumulation of Aβ(1-42) on gel phase domains of lipid bilayers: an AFM and fluorescence study
    • Choucair A., Chakrapani M., Chakravarthy B., Katsaras J., and Johnston L.J. Preferential accumulation of Aβ(1-42) on gel phase domains of lipid bilayers: an AFM and fluorescence study. Biochim. Biophys. Acta 1768 (2007) 146-154
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 146-154
    • Choucair, A.1    Chakrapani, M.2    Chakravarthy, B.3    Katsaras, J.4    Johnston, L.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.