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SELF-ASSEMBLING OF NEUTRAL AND CHARGED NANOPARTICLES INTO CORE-SHELL NANOHYBRIDS THROUGH HETEROAGGREGATION WITH SIZE CONTROL
Title
SELF-ASSEMBLING OF NEUTRAL AND CHARGED NANOPARTICLES INTO CORE-SHELL NANOHYBRIDS THROUGH HETEROAGGREGATION WITH SIZE CONTROL.
Creator
Hussain, Kazi Albab, Yi, Peng, Florida Atlantic University, College of Engineering and Computer Science, Department of Civil, Environmental and Geomatics Engineering
Abstract/Description
Core-shell nanohybrids have wide applications in pollutant degradation. In this study, core-shell nanohybrid was formed through heteroaggregation between neutral nanoparticles (i.e., hematite nanoparticles or HemNPs) and charged nanoparticles (i.e., carboxylated polystyrene nanoparticles or PSNPs). In the dispersant solution of 1 mM NaCl at pH 6.3, HemNPs were neutral and underwent favorable homoaggregation, whereas PSNPs were negatively charged and underwent no homoaggregation. When the two...
Show moreCore-shell nanohybrids have wide applications in pollutant degradation. In this study, core-shell nanohybrid was formed through heteroaggregation between neutral nanoparticles (i.e., hematite nanoparticles or HemNPs) and charged nanoparticles (i.e., carboxylated polystyrene nanoparticles or PSNPs). In the dispersant solution of 1 mM NaCl at pH 6.3, HemNPs were neutral and underwent favorable homoaggregation, whereas PSNPs were negatively charged and underwent no homoaggregation. When the two types of particles were mixed, homoaggregation of HemNPs and heteroaggregation between HemNPs and PSNPs took place simultaneously, forming HemNPs-PSNPs heteroaggregates. The transmission electron microscopy images of heteroaggregates show that HemNPs and PSNPs formed core-shell structure in which HemNPs were the cores and PSNPs were the shells. The size of the core-shell nanohybrids can be controlled by varying the concentration ratio of HemNPs to PSNPs. The increase of the size of charged nanoparticles resulted in larger nanohybrids. This new method has lower energy footprint than existing ones.
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Date Issued
2019
PURL
http://purl.flvc.org/fau/fd/FA00013317
Subject Headings
Nanoparticles, Core-shell structures, Nanohybrids, Aggregation (Chemistry)
Format
Document (PDF)
Effects of small molecule modulators and Phospholipid Liposomes on βeta-amyloid (1-40) Amyloidogenesis
Title
Effects of small molecule modulators and Phospholipid Liposomes on βeta-amyloid (1-40) Amyloidogenesis.
Creator
Morris, Clifford, Du, Deguo, Florida Atlantic University, Charles E. Schmidt College of Science, Department of Chemistry and Biochemistry
Abstract/Description
Beta-Amyloid (1-40) (Aβ40) is an aggregation prone protein, which undergoes a nucleation-dependent aggregation process causing the pathological neurodegeneration by amyloid plaque formation implicated in Alzheimer’s disease. In this thesis, we investigated the effects of small molecule modulators extracted from the marine invertebrate Pseudopterogorgia elisabethae on the Aβ40 amyloidogenic process using in- vitro ThT fluorescence assay and atomic force microscopy. We also investigated the...
Show moreBeta-Amyloid (1-40) (Aβ40) is an aggregation prone protein, which undergoes a nucleation-dependent aggregation process causing the pathological neurodegeneration by amyloid plaque formation implicated in Alzheimer’s disease. In this thesis, we investigated the effects of small molecule modulators extracted from the marine invertebrate Pseudopterogorgia elisabethae on the Aβ40 amyloidogenic process using in- vitro ThT fluorescence assay and atomic force microscopy. We also investigated the effects of neutral and anionic phospholipid liposomes on Aβ40 aggregation. Our results show that a marine natural product Pseudopterosin-A and its derivatives can suppress and modulate the Aβ40 aggregation process. Furthermore, our results demonstrate that a neutral phospholipid liposome inhibits Aβ40 fibril formation, whereas the anionic liposomes promote it.
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Date Issued
2015
PURL
http://purl.flvc.org/fau/fd/FA00004453, http://purl.flvc.org/fau/fd/FA00004453
Subject Headings
Aggregation (Chemistry), Alzheimer's disease -- Pathogenesis, Alzheimer's disease -- Research, Amyloid beta protein, Molecular biology, Molecular dynamics, Prions, Proteins -- Metabolism -- Disorders
Format
Document (PDF)