A5030419195- Alzheimer's disease research and treatments
- Advanced Fluorescence Microscopy Techniques
- Parkinson's Disease Mechanisms and Treatments
- Neuroinflammation and Neurodegeneration Mechanisms
- Prion Diseases and Protein Misfolding
- Biotin and Related Studies
- Fungal and yeast genetics research
- Supramolecular Self-Assembly in Materials
- Attention Deficit Hyperactivity Disorder
- Probiotics and Fermented Foods
- Fungal Biology and Applications
- Mycorrhizal Fungi and Plant Interactions
- Cell death mechanisms and regulation
- Bacterial Genetics and Biotechnology
- interferon and immune responses
- Transgenic Plants and Applications
- Nerve injury and regeneration
- Surfactants and Colloidal Systems
- Botulinum Toxin and Related Neurological Disorders
- Proteins in Food Systems
- Antifungal resistance and susceptibility
- Lipid Membrane Structure and Behavior
- Immune cells in cancer
- Monoclonal and Polyclonal Antibodies Research
- Nuclear Receptors and Signaling
The University of Sydney
2018-2024
Abstract Protein misfolding and aggregation into oligomeric fibrillar structures is a common feature of many neurogenerative disorders. Single‐molecule techniques have enabled characterization these lowly abundant, highly heterogeneous protein aggregates, previously inaccessible using ensemble averaging techniques. However, they usually rely on the use recombinantly‐expressed labeled protein, or addition amyloid stains that are not protein‐specific. To circumvent challenges, we made high...
Abstract Background Widescale evidence points to the involvement of glia and immune pathways in progression Alzheimer’s disease (AD). AD-associated iPSC-derived glial cells show a diverse range AD-related phenotypic states encompassing cytokine/chemokine release, phagocytosis morphological profiles, but date studies are limited derived from PSEN1, APOE APP mutations or sporadic patients. The aim current study was successfully differentiate microglia astrocytes patients harbouring an...
The central hallmark of Parkinson's disease pathology is the aggregation α-synuclein protein, which, in its healthy form, associated with lipid membranes. Purified monomeric relatively stable vitro, but can be triggered by presence vesicles. Despite this importance lipids context aggregation, their detailed mechanistic role process has not been established to date. Here, we use chemical kinetics develop a model that able globally describe behaviour DMPS vesicles, across range and protein...
Protein misfolding and aggregation is a characteristic of many neurodegenerative disorders, including Alzheimer's Parkinson's disease. The oligomers generated during are likely involved in disease pathogenesis present promising biomarker candidates. However, owing to their small size low concentration, specific tools quantify characterize aggregates complex biological samples still lacking. Here, we single-molecule two-color aggregate pulldown (STAPull), which overcomes this challenge by...
Fluorescent probes for biological imaging have revealed much about the functions of biomolecules in health and disease. Fluorogenic probes, which are fluorescent only upon a bioorthogonal reaction with specific partner, particularly advantageous as they ensure that signals observed arise solely from intended target. In this work, we report first series naphthalimide tetrazines fluorogenic labelling. We establish all these compounds can be used through photophysical, analytical studies. The...
TIR-domain-containing adapter-inducing interferon-β (TRIF) is an innate immune protein that serves as adaptor for multiple cellular signalling outcomes in the context of infection. TRIF activated via ligation Toll-like receptors 3 and 4. One outcome TRIF-directed activation programmed cell death pathway necroptosis, which governed by interactions between proteins contain a RIP Homotypic Interaction Motif (RHIM). contains RHIM sequence can interact with receptor interacting kinases 1 (RIPK1)...
Many soluble proteins can self-assemble into macromolecular structures called amyloids, a subset of which are implicated in range neurodegenerative disorders. The nanoscale size and structural heterogeneity prefibrillar early aggregates, as well mature amyloid fibrils, pose significant challenges for the quantification morphologies. We report fluorescent sensor AmyBlink-1 its application super-resolution imaging structures. exhibits 5-fold increase ratio green (thioflavin T) to red (Alexa...
Hydrophobins are remarkable proteins due to their ability self-assemble into amphipathic coatings that reverse surface wettability. Here, the versatility of Class I hydrophobins EASΔ15 and DewY in diverse nanosuspension coating applications is demonstrated. The shown coat or emulsify a range substrates including oil, hydrophobic drugs, nanodiamonds alter solution behavior. Surprisingly, while confer new properties, only subset found be resistant hot detergent treatment, feature previously...
Abstract Many soluble proteins can self‐assemble into macromolecular structures called amyloids, a subset of which are implicated in range neurodegenerative disorders. The nanoscale size and structural heterogeneity prefibrillar early aggregates, as well mature amyloid fibrils, pose significant challenges for the quantification morphologies. We report fluorescent sensor AmyBlink‐1 its application super‐resolution imaging structures. exhibits 5‐fold increase ratio green (thioflavin T) to red...
Protein misfolding and aggregation into oligomeric fibrillar structures is a common feature of many neurogenerative disorders. Single-molecule techniques have enabled characterization these lowly abundant, highly heterogeneous protein aggregates, previously inaccessible using ensemble averaging techniques. However, they usually rely on the use recombinantly-expressed labeled protein, or addition amyloid stains that are not protein-specific. To circumvent challenges, we made high affinity...
The central hallmark of Parkinson’s disease pathology is the aggregation α -synuclein protein, which, in its healthy form, associated with lipid membranes. Purified monomeric relatively stable vitro, but can be triggered by presence vesicles. Despite this importance lipids context aggregation, their mechanistic role process has not been established to date. Here, we use chemical kinetics develop a detailed model that able globally describe behaviour DMPS vesicles, across range and protein...
Abstract Background Widescale evidence points to the involvement of glia and immune pathways in progression Alzheimer’s disease (AD). AD-associated iPSC-derived glial cells show a diverse range AD-related phenotypic states encompassing cytokine/chemokine release, phagocytosis morphological profiles, but date studies are limited derived from PSEN1, APOE APP mutations or sporadic patients. The aim current study was successfully differentiate microglia astrocytes patients harbouring an...
Alzheimer's disease is imposing a growing social and economic burden worldwide, effective therapies are urgently required. One possible approach to modulation of the outcome use small molecules limit conversion monomeric amyloid (Aβ42) cytotoxic oligomers fibrils. We have synthesized modulators assembly that unlike others studied date: these compounds act primarily by sequestering Aβ42 monomer. provide kinetic nuclear magnetic resonance data showing perphenazine conjugates divert monomer...
Abstract The misfolding and aggregation of protein is a characteristic many neurodegenerative disorders, including Alzheimer’s Parkinson’s disease. wide range sizes structures oligomers fibrils generated have previously been studied using single-molecule super-resolution microscopy. These methods, however, tend to rely on the use either directly labeled protein, or addition non-specific amyloid stains, such as thioflavin-T. This has prevented characterization aggregate composition in complex...
Abstract Alzheimer’s disease is imposing a growing social and economic burden worldwide effective therapies are required. Strategies aimed at the removal of fibrillar plaques formed by amyloid-β peptide have not proved therapeutic focus has shifted to approaches that target cytotoxic oligomeric species populated before fibrils deposited. We designed synthesized perphenazine-cyclam conjugates specifically rapidly bind monomeric form Aβ42, reducing production both oligomers amyloid fibrils....
Many soluble proteins can self-assemble into macromolecular structures called amyloids, a subset of which are implicated in range neurodegenerative disorders. The nanoscale size and structural heterogeneity prefibrillar early aggregates, as well mature amyloid fibrils, pose significant challenges for the quantification species, identification their cellular interaction partners elucidation molecular basis cytotoxicity. We report fluorescent sensor AmyBlink-1 its application super-resolution...
Many soluble proteins can self-assemble into macromolecular structures called amyloids, a subset of which are implicated in range neurodegenerative disorders. The nanoscale size and structural heterogeneity prefibrillar early aggregates, as well mature amyloid fibrils, pose significant challenges for the quantification species, identification their cellular interaction partners elucidation molecular basis cytotoxicity. We report fluorescent sensor AmyBlink-1 its application super-resolution...