Impact of the Morphology of Molybdenum Disulfide on Inhibition of Bovine Insulin Fibrillation
碩士 === 國立中山大學 === 化學系研究所 === 106 === MoS2 nanosheets (MoS2 NSs) have been shown in past publication having various advantages: easily uptake by cells, surface modification of functional groups and low cytotoxicity, with high degradability (in vivo). In recent studies, in order to increase the disper...
Main Authors: | , |
---|---|
Other Authors: | |
Format: | Others |
Language: | zh-TW |
Published: |
2018
|
Online Access: | http://ndltd.ncl.edu.tw/handle/aj5526 |
id |
ndltd-TW-106NSYS5065021 |
---|---|
record_format |
oai_dc |
spelling |
ndltd-TW-106NSYS50650212019-10-31T05:22:28Z http://ndltd.ncl.edu.tw/handle/aj5526 Impact of the Morphology of Molybdenum Disulfide on Inhibition of Bovine Insulin Fibrillation 二硫化鉬型態對牛胰島素纖維化調控抑制之影響 Song-hao Huang 黃嵩皓 碩士 國立中山大學 化學系研究所 106 MoS2 nanosheets (MoS2 NSs) have been shown in past publication having various advantages: easily uptake by cells, surface modification of functional groups and low cytotoxicity, with high degradability (in vivo). In recent studies, in order to increase the dispersion of MoS2 nanosheets in water, the molecules used as dispersions have evolved from commercial surfactants to biomolecules, such as lysozymes, bovine serum albumin, silk fibroin, etc., which are suitable for organisms. This phenomenon shows that the MoS2 nanosheets have a strong affinity for the peptide molecules in vivo. Amyloid diseases: including Alzheimer''s, Parkinson''s and type 2 diabetes each have their own pathologies associated with specific amyloidogenic peptides or proteins. The fibrosis of each of these peptides involves complex multi-steps. The process changes from monomeric form to soluble oligomers and fibril or amyloid seed until eventually large hydrophobic mature fibrils are formed. Current research supports low molecular weight soluble oligomers as an intermediate species in the aggregation pathway that ultimately contributes to amyloid-mediated cell death. Therefore, many studies using small molecule drugs or nanomaterials to control amyloid inhibition have flourished. As described in the previous paragraph, this study performed a series of studies on the affinity between molybdenum disulfide nanosheets and bovine insulin, and the regulation of bovine insulin aggregation. The theoretical calculation of affinity shows that the negatively charged and hydrophobic nature of MoS2 nanosheets surface facilitates the adsorption of positively charged and hydrophobic amino acids. Different sizes of molybdenum disulfide nanoparticles were prepared at different ultrasonic oscillation times, and the best size was selected in experiments that inhibit bovine insulin aggregation. Finally, it is concluded that the MoS2 nanosheets help to reduce the formation of bovine insulin fibers and reduce the resulting hemolytic effects, will expand the application value of MoS2 nanosheets in biochemistry. Wei-Lung Tseng 曾韋龍 2018 學位論文 ; thesis 54 zh-TW |
collection |
NDLTD |
language |
zh-TW |
format |
Others
|
sources |
NDLTD |
description |
碩士 === 國立中山大學 === 化學系研究所 === 106 === MoS2 nanosheets (MoS2 NSs) have been shown in past publication having various advantages: easily uptake by cells, surface modification of functional groups and low cytotoxicity, with high degradability (in vivo). In recent studies, in order to increase the dispersion of MoS2 nanosheets in water, the molecules used as dispersions have evolved from commercial surfactants to biomolecules, such as lysozymes, bovine serum albumin, silk fibroin, etc., which are suitable for organisms. This phenomenon shows that the MoS2 nanosheets have a strong affinity for the peptide molecules in vivo.
Amyloid diseases: including Alzheimer''s, Parkinson''s and type 2 diabetes each have their own pathologies associated with specific amyloidogenic peptides or proteins. The fibrosis of each of these peptides involves complex multi-steps. The process changes from monomeric form to soluble oligomers and fibril or amyloid seed until eventually large hydrophobic mature fibrils are formed. Current research supports low molecular weight soluble oligomers as an intermediate species in the aggregation pathway that ultimately contributes to amyloid-mediated cell death. Therefore, many studies using small molecule drugs or nanomaterials to control amyloid inhibition have flourished. As described in the previous paragraph, this study performed a series of studies on the affinity between molybdenum disulfide nanosheets and bovine insulin, and the regulation of bovine insulin aggregation. The theoretical calculation of affinity shows that the negatively charged and hydrophobic nature of MoS2 nanosheets surface facilitates the adsorption of positively charged and hydrophobic amino acids. Different sizes of molybdenum disulfide nanoparticles were prepared at different ultrasonic oscillation times, and the best size was selected in experiments that inhibit bovine insulin aggregation.
Finally, it is concluded that the MoS2 nanosheets help to reduce the formation of bovine insulin fibers and reduce the resulting hemolytic effects, will expand the application value of MoS2 nanosheets in biochemistry.
|
author2 |
Wei-Lung Tseng |
author_facet |
Wei-Lung Tseng Song-hao Huang 黃嵩皓 |
author |
Song-hao Huang 黃嵩皓 |
spellingShingle |
Song-hao Huang 黃嵩皓 Impact of the Morphology of Molybdenum Disulfide on Inhibition of Bovine Insulin Fibrillation |
author_sort |
Song-hao Huang |
title |
Impact of the Morphology of Molybdenum Disulfide on Inhibition of Bovine Insulin Fibrillation |
title_short |
Impact of the Morphology of Molybdenum Disulfide on Inhibition of Bovine Insulin Fibrillation |
title_full |
Impact of the Morphology of Molybdenum Disulfide on Inhibition of Bovine Insulin Fibrillation |
title_fullStr |
Impact of the Morphology of Molybdenum Disulfide on Inhibition of Bovine Insulin Fibrillation |
title_full_unstemmed |
Impact of the Morphology of Molybdenum Disulfide on Inhibition of Bovine Insulin Fibrillation |
title_sort |
impact of the morphology of molybdenum disulfide on inhibition of bovine insulin fibrillation |
publishDate |
2018 |
url |
http://ndltd.ncl.edu.tw/handle/aj5526 |
work_keys_str_mv |
AT songhaohuang impactofthemorphologyofmolybdenumdisulfideoninhibitionofbovineinsulinfibrillation AT huángsōnghào impactofthemorphologyofmolybdenumdisulfideoninhibitionofbovineinsulinfibrillation AT songhaohuang èrliúhuàmùxíngtàiduìniúyídǎosùxiānwéihuàdiàokòngyìzhìzhīyǐngxiǎng AT huángsōnghào èrliúhuàmùxíngtàiduìniúyídǎosùxiānwéihuàdiàokòngyìzhìzhīyǐngxiǎng |
_version_ |
1719284452606083072 |