Interaction of BetaAmyloid with Membrane Investigated by Fluorescence Spectroscopy

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68407700%3A21460%2F13%3A00213729" target="_blank" >RIV/68407700:21460/13:00213729 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Interaction of BetaAmyloid with Membrane Investigated by Fluorescence Spectroscopy
Original language description
Alzheimer?s disease is linked to the misfolding and aggregation of beta-amyloid (A?) peptides. The main mechanism of pathogenesis and the conditions which lead to uncontrolled self-assembly are unfortunately to this date not fully understood. Interactionof beta-amyloid with the neuronal membrane surface has been implicated to be a possible source of cytotoxicity. The objective of this thesis is the application of both time-resolved fluorescence spectroscopy and steady-state fluorescence spectroscopy tomonitor beta-amyloid aggregation and interactions with model biological membranes. A novel approach of monitoring beta-amyloid aggregation using the fluorescence lifetime of the dye Thioflavin T was employed. The experimental results bring new insightson fluorescence properties of Thioflavin T and on the utilisation of the dye for assessing the process of amyloid aggregation. The interaction of beta-amyloid with model membranes was studied via several spectroscopic methods using an env
Czech name
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Czech description
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Project
<a href="/en/project/EE.2.3.20.0092" target="_blank" >EE.2.3.20.0092: BIO-XUV Research Team Advancement at FBME CTU</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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