Circular Dichroism Spectroscopic Study of b-Amyloid Aggregation and the Effects of Inhibitors | POSTER
Introduction
Neurodegenerative disorders, including Alzheimer’s disease (AD) and Parkinson’s disease (PD), are characterized by progressive cognitive decline, and global efforts are underway to develop effective treatments. Key proteins such as β-amyloid, 1 a-synuclein, and tau are implicated in the pathogenesis of these diseases. the aggregation of β-amyloid plays a central role in neurodegenerative diseases such as AD, and research on this phenomenon is crucial for understanding the pathology and developing therapeutic strategies. β-amyloid exists extracellularly and undergoes an aggregation process, in which monomeric peptides form micellar intermediates under certain stimuli, which then further grow into fibrils (fibrous structures) or form amyloid plaques. These amyloid plaques accumulate between neurons, and ultimately lead to neuronal death. Understanding this aggregation process is essential for discovering new approaches to prevent or treat the disease. Circular dichroism (CD) spectroscopy is well known as a convenient and sensitive method for investigating the higher-order structure (HOS) of proteins in solution. This technique can monitor the changes in HOS and the formation of aggregates by measuring CD signals of β-amyloid peptide,2-4 making it valuable for elucidating disease mechanisms and advancing the development of effective therapeutics and preventive agents. In this presentation, we report the results of the evaluation of the performance of ionic liquids as inhibitors of amyloid aggregate formation and as solubilizers of β-amyloid peptide aggregates using CD spectroscopy and the BeStSel program, which allows accurate and detailed evaluation of secondary structure of proteins.
References
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