Kinetics and Thermodynamics of Liposome & ß-amyloid Interactions by Surface Plasmon Resonance and Isothermal Titration Microcalorimetry
碩士 === 國立中央大學 === 化學工程與材料工程研究所 === 93 === ß-amyloid（Aß）was believed to cause the prime factor of Alzheimer’s disease. However, the mechanism of the cytotoxicity and the disease caused by Aß is still unclear. The goal of this work is to study the interactions of various incubated time of Aß with desi...
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| Format: | Others |
| Language: | zh-TW |
| Published: |
2005
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| Online Access: | http://ndltd.ncl.edu.tw/handle/99063054131892038463 |
| Summary: | 碩士 === 國立中央大學 === 化學工程與材料工程研究所 === 93 === ß-amyloid（Aß）was believed to cause the prime factor of Alzheimer’s disease. However, the mechanism of the cytotoxicity and the disease caused by Aß is still unclear. The goal of this work is to study the interactions of various incubated time of Aß with designed liposomes. The objective of this investigation was achived by the following studies : The structural and aggrergation information of Aß by by circular dichroism spectroscopy（CD）, by Thioflavin T fluorescence assay and monitored by atomic force microscopy（AFM）. Futhermore, this investigation utilized surface plasmon resonance (SPR) and isothermal titration microcalorimetry (ITC) to measure the kinetics and binding enthalpy of Aß with the liposomes.
Kinetics of interactions of Aß and liposomes by SPR reveal the driving force of fresh Aß interacts with various liposomes is electrostatics. And fresh Aß have high affinity with GM1. Addition of cholesterol to the liposome could alter membrane fluidity and affect the interactions of fresh Aß with liposomes especially in the amount of absorbed Aß and maintained the structure of liposome after adsorbing. The driving force of the 1 day of incubation of Aß interacts with various liposomes is hydrophobicity. The binding enthalpy measurements between Aß and liposomes by ITC are endothermic reaction. When the composition of liposome is zwitterionic lipids, the interaction of Aß with liposomes is predominantly hydrophobic force; in contrast with the drive force of interaction of charged lipid with Aß is electrostatic force.
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