Contribution in an anthology

Appeared in: Alzheimer’s Disease : Cellular and Molecular Aspects of Amyloid β

Editor list: Harris, JR; Fahrenholz, F

Publication year: 2005

Pages: 319-337

ISBN: 978-0-387-23225-6

eISBN: 978-0-387-23226-3

DOI Link: https://doi.org/10.1007/0-387-23226-5_16

Title of series: Subcellular Biochemistry

Number in series: 38

Abstract: 

The interaction of Aβ with synaptosomal plasma membranes decreases membrane fluidity. Using model membrane/Iiposome systems the interaction of Aβ with specific lipids (e.g. phospholipids, gangliosides, cholesterol) has been defined. The formation of the β-sheet structure of Aβ when undergoing peptide aggregation is important for Aβ’s membrane perturbing properties. This effect can be correlated with the peptide length of Aβ, the longer Aβ_1-42 having the greatest effect on membrane fluidity and on neurotoxicity.

Harvard Citation style: Eckert, G., Wood, W. and Müller, W. (2005) Membrane Disordering Effects of β-Amyloid Peptides, in Harris, J. and Fahrenholz, F. (eds.) Alzheimer’s Disease : Cellular and Molecular Aspects of Amyloid β. New York: Springer, pp. 319-337. https://doi.org/10.1007/0-387-23226-5_16

APA Citation style: Eckert, G., Wood, W., & Müller, W. (2005). Membrane Disordering Effects of β-Amyloid Peptides. In Harris, J., & Fahrenholz, F. (Eds.), Alzheimer’s Disease : Cellular and Molecular Aspects of Amyloid β (pp. 319-337). Springer. https://doi.org/10.1007/0-387-23226-5_16