Control of Amyloid Aggregation by Applying Gold Nanoparticles and Metal Ions

碩士 === 國立臺灣科技大學 === 化學工程系 === 104 === In our study, we use the gold nanoparticles and different metal ions to control the formation of amyloid fiber structure of the neurodegenerative diseases (like as huntingtin’s disease (HD) and amyotrophic lateral sclerosis (ALS)). There are two part in my disse...

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Main Authors: Yu-Cai Chen, 陳育材
Other Authors: Jen-Tse Huang
Format: Others
Language:zh-TW
Published: 2016
Online Access:http://ndltd.ncl.edu.tw/handle/85932234191339239523
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spelling ndltd-TW-104NTUS53420192017-09-03T04:25:30Z http://ndltd.ncl.edu.tw/handle/85932234191339239523 Control of Amyloid Aggregation by Applying Gold Nanoparticles and Metal Ions 應用特殊修飾金奈米粒子與金屬離子控制類澱粉樣纖維之生長 Yu-Cai Chen 陳育材 碩士 國立臺灣科技大學 化學工程系 104 In our study, we use the gold nanoparticles and different metal ions to control the formation of amyloid fiber structure of the neurodegenerative diseases (like as huntingtin’s disease (HD) and amyotrophic lateral sclerosis (ALS)). There are two part in my dissertation, part A is based on the rational designed amyloid-sensitive gold nanoparticles (AuNPs) to apply in huntingtin’s disease and we use the KKQ20K as the model study of huntingtin’s disease. By the result of the UV/Vis spectroscopy, the X-ray photoelectron spectroscopy (XPS) and the transmission electron microscopy (TEM), indicating the AuNPs can prevent the formation of KKQ20K amyloid aggregation, and the TEM image also showing that AuNPs have the ability to destroy the fiber form of KKQ20K. On the other hand, we co-incubated the AuNPs with another peptide of the neurodegenerative diseases demonstrate that the AuNPs can affinity to interact with the polyglutamine (polyQ)-rich peptide. In cell study, we choose the eYFP-tagged mutant Huntingtin (109Q) protein to do the experiment. In order to increase the uptake of cell, we coating a polyethyleneimine (PEI) layer on the surface of AuNPs. From the cell study, showing that the AuNPs can dissociate the large cytosolic aggregates. In the part B, we use the different metal ions co-incubation with D1 and QN1 of the c-terminal in TAR DNA-binding protein 43 of ALS. In the result of the circular dichroism spectrum and the fluorescence spectrometry show that, for QN1, zinc ion cause more and stronger β-sheet structure, copper ion result in forming amorphous aggregates, and the influence of aluminum ion was slightly. For D1, copper ion will accelerate the aggregation, and conversely aluminum ion cause D1 maintain random coil signal of CD spectrum. The huge difference between the QN1 and D1 affected metal ions, maybe is due to the sequence causing the stacking structure and the interaction with metal ions are very different. This hypothesis will be prove by further analysis. Jen-Tse Huang Ming-Hua Ho 黃人則 何明樺 2016 學位論文 ; thesis 131 zh-TW
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description 碩士 === 國立臺灣科技大學 === 化學工程系 === 104 === In our study, we use the gold nanoparticles and different metal ions to control the formation of amyloid fiber structure of the neurodegenerative diseases (like as huntingtin’s disease (HD) and amyotrophic lateral sclerosis (ALS)). There are two part in my dissertation, part A is based on the rational designed amyloid-sensitive gold nanoparticles (AuNPs) to apply in huntingtin’s disease and we use the KKQ20K as the model study of huntingtin’s disease. By the result of the UV/Vis spectroscopy, the X-ray photoelectron spectroscopy (XPS) and the transmission electron microscopy (TEM), indicating the AuNPs can prevent the formation of KKQ20K amyloid aggregation, and the TEM image also showing that AuNPs have the ability to destroy the fiber form of KKQ20K. On the other hand, we co-incubated the AuNPs with another peptide of the neurodegenerative diseases demonstrate that the AuNPs can affinity to interact with the polyglutamine (polyQ)-rich peptide. In cell study, we choose the eYFP-tagged mutant Huntingtin (109Q) protein to do the experiment. In order to increase the uptake of cell, we coating a polyethyleneimine (PEI) layer on the surface of AuNPs. From the cell study, showing that the AuNPs can dissociate the large cytosolic aggregates. In the part B, we use the different metal ions co-incubation with D1 and QN1 of the c-terminal in TAR DNA-binding protein 43 of ALS. In the result of the circular dichroism spectrum and the fluorescence spectrometry show that, for QN1, zinc ion cause more and stronger β-sheet structure, copper ion result in forming amorphous aggregates, and the influence of aluminum ion was slightly. For D1, copper ion will accelerate the aggregation, and conversely aluminum ion cause D1 maintain random coil signal of CD spectrum. The huge difference between the QN1 and D1 affected metal ions, maybe is due to the sequence causing the stacking structure and the interaction with metal ions are very different. This hypothesis will be prove by further analysis.
author2 Jen-Tse Huang
author_facet Jen-Tse Huang
Yu-Cai Chen
陳育材
author Yu-Cai Chen
陳育材
spellingShingle Yu-Cai Chen
陳育材
Control of Amyloid Aggregation by Applying Gold Nanoparticles and Metal Ions
author_sort Yu-Cai Chen
title Control of Amyloid Aggregation by Applying Gold Nanoparticles and Metal Ions
title_short Control of Amyloid Aggregation by Applying Gold Nanoparticles and Metal Ions
title_full Control of Amyloid Aggregation by Applying Gold Nanoparticles and Metal Ions
title_fullStr Control of Amyloid Aggregation by Applying Gold Nanoparticles and Metal Ions
title_full_unstemmed Control of Amyloid Aggregation by Applying Gold Nanoparticles and Metal Ions
title_sort control of amyloid aggregation by applying gold nanoparticles and metal ions
publishDate 2016
url http://ndltd.ncl.edu.tw/handle/85932234191339239523
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