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| Azobenzénové deriváty ako potenciálne terapeutiká pre Alzheimerovu chorobu | |
| Azobenzenes as potential Alzheimer\’s theranostic agents | |
| Program: | Mobility |
| Project leader: | RNDr. Bednáriková Zuzana, PhD. |
| Annotation: | Amyloid fibrils of amyloid β (Aβ) peptides are a neuropathological feature of Alzheimer\’s disease (AD). AD is one of the world\’s fastest-growing neurological diseases with substantial economic and societal impact, but no cure is currently available. Therefore, the exploration of novel treatment approaches is in high demand. The project\’s main objective is to study the ability of azobenzene molecules to affect targets associated with the amyloid cascade of AD pathogenesis. The project will employ the lever-like potential of azobenzene molecules to dissociate fibrillar aggregates of Aβ peptides and inhibit the proteolytic activity of β-secretase. We will integrate in vitro, in silico, and cells workflow to find a possible alternative therapy against this devastating disease. Moreover, this collaborative research partnership will present an excellent opportunity for both teams\’ young members to learn new techniques in the well-equipped laboratories at the Polish and Slovak Academies of Sciences and gain new experience by working in an international scientific environment. |
| Duration: | 1.1.2023 – 31.12.2024 |
National
| Objasnenie počiatočných štádií amyloidnej agregácie proteínov – od mechanizmu k terapii | |
| Unraveling the early events of protein amyloid aggregation – from mechanism to therapy | |
| Program: | VEGA |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | Structural changes of poly/peptides leading to the formation of amyloid aggregates are associated with incurablediseases, like Alzheimer\’s disease or diabetes. While the general mechanisms of fibril formation and theircharacterization are well reported, the early events during poly/peptide fibrillation are still unclear. The project isfocused on understanding the early events mechanisms leading to the formation of pre-fibrillar (partially un/foldedintermediates, nuclei, oligomers) and fibrillar amyloid aggregates of selected globular and intrinsically disorderedproteins. Our focus will be the study of the kinetics of pre-fibrillar structures formation, their morphology, andcytotoxicity, under various experimental conditions, and in the presence of selected interacting partners (smallmolecules, nanoparticles). The obtained results will contribute to understanding the early events of amyloidaggregation and identifying the inhibitors with therapeutic potential for amyloid diseases. |
| Duration: | 1.1.2021 – 31.12.2024 |