Several neurodegenerative disorders, such as Alzheimer's disease, are characterized by the accumulation of extracellular insoluble fibrillar aggregates that lead to synaptic dysfunction and nerve cell death. Compounds capable of binding and preventing Aβ peptide aggregation, such as flavonoids or epigallocatechin gallate, occur ubiquitously in plants and vegetables and exert neuroprotective effects. Since plant-derived extracts are rich in phenolic compounds, we have characterized by NMR and LC-HRMS various aqueous, alcoholic and hydro-alcoholic extracts of Myrtle leaves, searching for potential anti-amylodogenic compounds, as putative molecular tools for the prevention of neurodegenerative disorders. To better elucidate these mechanisms, large quantities of purified Aβ peptide are required. Here, we also present a first attempt to express and purify recombinant Aβ1-42 in E. coli, which could lead to satisfactory yield and purity.
Moretti, L., Palmioli, A., Regonesi, M., Ami, D., Natalello, A., Airoldi, C. (2024). Identification and characterization of anti-amyloidogenic natural compounds for the prevention of age-related neurodegenerative diseases. Intervento presentato a: TeCSBi PhD Meeting 2024, Milano, Italia.
Identification and characterization of anti-amyloidogenic natural compounds for the prevention of age-related neurodegenerative diseases
Moretti, L
;Palmioli, A;Regonesi, M;Ami, D;Natalello, A;Airoldi, C
2024
Abstract
Several neurodegenerative disorders, such as Alzheimer's disease, are characterized by the accumulation of extracellular insoluble fibrillar aggregates that lead to synaptic dysfunction and nerve cell death. Compounds capable of binding and preventing Aβ peptide aggregation, such as flavonoids or epigallocatechin gallate, occur ubiquitously in plants and vegetables and exert neuroprotective effects. Since plant-derived extracts are rich in phenolic compounds, we have characterized by NMR and LC-HRMS various aqueous, alcoholic and hydro-alcoholic extracts of Myrtle leaves, searching for potential anti-amylodogenic compounds, as putative molecular tools for the prevention of neurodegenerative disorders. To better elucidate these mechanisms, large quantities of purified Aβ peptide are required. Here, we also present a first attempt to express and purify recombinant Aβ1-42 in E. coli, which could lead to satisfactory yield and purity.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.


