Examination of the interactions between amyloid proteins and cell membrane
Date Issued
2005
Date
2005
Author(s)
Liu, Kuan-Nan
DOI
zh-TW
Abstract
Up to now, at least twenty different human proteins and peptides have been isolated as the fibrillar components of disease-associated amyloid deposits. These proteins undergo aberrant changes in structure and accumulate to form aggregated species which lead to the amyloidogenic diseases. β-amyloid peptide (Aβ), the principal protein of Alzheimer’s disease, is also one of them.
Previous studies showed that the interaction between Aβ and cell membrane is highly correlated to Aβ-elicited neurotoxicity. Several lines of evidence showed that the interaction between phospholipid membrane and Aβ might be associated with electrostatic-mediated forces or membrane fluidity. However, the detailed mechanism of this interaction remains largely unknown.
In this work, we proposed a hypothesis that there is a link between membrane dipole potential and Aβ-cell membrane interaction, which is considered to be the first step in the mechanism of Aβ-induced toxicity and wish to test this hypothesis. To pursue our goals, we employed a dual-wavelength ratiometric fluorescence method with aid of the potential-sensitive fluorescent dye. At the outset, we sought out the optimal experimental conditions of the aforementioned ratiometric method. Next, we investigated the effect of binding of amyloid proteins and phospholipid vesicle on membrane dipole potential. Our results indicated that a decrease in dipole potential was observed upon binding of aggregated amyloid proteins to phospholipid membrane. In addition, a more dramatic change in membrane dipole potential was detected in phospholipid vesicles with cholesterol. We believe that our outcome may contribute to a better understanding of the mechanism(s) associated with AD and other amyloid diseases.
Subjects
類澱粉症
偶極電位
阿滋海默症
amyloidosis
dipole potential
SDGs
Type
thesis
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