Driving force of binding of amyloid beta-protein to lipid bilayers.

Biochemical and biophysical research communications (2008-04-09)
Keisuke Ikeda, Katsumi Matsuzaki
ABSTRACT

Amyloid beta-protein (Abeta) has been reported to interact with a variety of lipid species, although the thermodynamic driving force remains unclear. We investigated the binding of Abetas labeled with the dye diethylaminocoumarin (DAC-Abetas) to lipid bilayers under various conditions. DAC-Abeta-(1-40) electrostatically bound to anionic and cationic lipids at acidic and alkaline interfacial pH, respectively. However, at neutral pH, electroneutral Abeta did not bind to these lipids, indicating little hydrophobic interaction between Abeta-(1-40) and the acyl chains of lipids. In contrast, DAC-Abeta associated with glycolipids even under electroneutral conditions. These results suggested that hydrogen-bonding as well as hydrophobic interactions with sugar groups of glycolipids drive the membrane binding of Abeta-(1-40).

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
7-(Diethylamino)coumarin-3-carboxylic acid, BioReagent, suitable for fluorescence, ≥98.0% (HPCE)

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

MilliporeSigma

Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.