Oxana KlementievaSenior Lecturer, PhD
Research areas and keywords
UKÄ subject classification
- Medical and Health Sciences
- Medical and Health Sciences, Neurodegenerative diseases, Protein aggregation, Microspectroscopy
Abnormal aggregation of proteins in brain during the course of Alzheimer’s disease and Parkinson’s disease
Ageing of the world’s population has amplified neurodegenerative disorders, of which Alzheimer’s disease (AD) and Parkinson’s disease (PD) are the most common. Worldwide, nearly 44 million people have Alzheimer’s or a related dementia, and an estimated seven to ten million people have Parkinson’s disease. Both disorders are characterized by the presence of β-sheet enriched aggregates formed by of amyloid proteins, the subsequent damage and loss of neurons, as well as substantial synaptic degradation. AD displays aggregates of insoluble amyloid beta-protein. PD displays aggregates of insoluble α-synuclein. However, the molecular mechanism (or mechanisms) leading to the abnormal accumulation of Aβ and α‑syn remains unknown and as a result, the pathologies of these diseases are poorly understood, and at present there is no effective cure for neurodegenerative memory impairment.
Using infrared microspectroscopy, we are developing ultra-sensitive protocols to study amyloid protein aggregation in brain tissue. We pioneered novel and ground-breaking evidence of presymptomatic β-sheet enriched aggregates which appear before plaque and memory decline. Now MMS research team wants to understand why malignant protein aggregation begins in the brain and how these aggregated proteins spread in the brain.
To investigate the mutual effects of α-synuclein, amyloid-β and tau aggregation, we co-use traditional cellular biology approaches and synchrotron-based microspectroscopy techniques.
Recent research outputs
Research output: Contribution to journal › Article
Research output: Contribution to journal › Review article