Aurone derivatives assessment serves as proprietary probes of β amyloid aggregates in comparison with amorphous aggregates

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Título:
Aurone derivatives assessment serves as proprietary probes of β amyloid aggregates in comparison with amorphous aggregates
Autor: Abbasbeigi, Sirvan
Assuntos: Basic Pharmacology ; Biochemistry ; Biochemistry and Cell Biology not elsewhere classified ; Bioinformatics ; Bioinorganic Chemistry ; Biological Sciences not elsewhere classified ; Biological Techniques ; Biomarkers ; Biomolecular Modelling and Design ; Biophysics ; Biotechnology ; Cheminformatics ; Clinical Chemistry (diagnostics) ; Clinical Pharmacology and Therapeutics ; Computational Biology ; Developmental Biology ; Diseases ; FOS: Basic medicine ; FOS: Biological sciences ; FOS: Chemical sciences ; FOS: Clinical medicine ; FOS: Computer and information sciences ; Macromolecular and Materials Chemistry not elsewhere classified ; Medical Biochemistry and Metabolomics not elsewhere classified ; Medical Biochemistry: Inorganic Elements and Compounds ; Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics) ; Molecular Biology ; Molecular Medicine ; Pharmacology ; Physiology ; Protein Trafficking ; Proteomics and Intermolecular Interactions (excl. Medical Proteomics) ; Structural Biology (incl. Macromolecular Modelling) ; Synthetic Biology
Descrição: Objective: In 1854, the term “amyloid” was used for the first time by Virchow. To describe an aggregated substance found in the liver of a deceased patient. Despite the misleading association to starch, the term is still used a currently 27 diseases are associated with amyloid fibril deposits of normally soluble proteins. Early detection of amyloid deposits could be effective in the diagnosis and treatment of disorders such as Alzheimer’s disease (AD), Parkinson’s disease (PD), and systemic amyloidosis. In this study, we tried to synthesize the aurone derivatives as an amyloid detection probe to compare with a standard probe called Thioflavin T in the different protein conditions. Material and Methods: β-Lactogluboline was purified via fractionation method (As an all β secondary structure) and bovine serum albumin (As an α/β secondary structure) was purchased from Sigma Aldrich. For more precision, their qualities were evaluated by SDS-PAGE and Bradford protein assay. Furthermore, the spectrophotometric analysis of synthetic compounds such as UV-visible and fluorescence spectroscopies were considered in their individual and special wavelengths. Each synthetic compound was excited and the emission spectra were recorded immediately at their own exclusive wavelengths, while, they were bound to the amyloid fibrils in comparison with native protein and also amorphous aggregates. Results: The results of synthetic compounds were obtained in three different conditions, Native, Amorphous and Amyloid aggregations. We have shown that the synthetic compounds could selectively and specifically bind to amyloid fibrils almost as much as the ThT probe. Additionally, our synthetic compounds due to its neutral charge and high lipophilicity essence might cross the blood-brain barrier as an effective probe. Conclusion: According to our result, the synthetic compounds could be accounted as remarkable probes to detect in vitro β-amyloid plaques, but it should be investigated further as potential probes for detecting β-amyloid plaques in the AD brain.
Editor: figshare
Data de criação/publicação: 2021
Idioma: Inglês

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Aurone derivatives assessment serves as proprietary probes of β amyloid aggregates in comparison with amorphous aggregates

Abbasbeigi, Sirvan

figshare 2021

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