Liquid-phase electron microscopy studies of Amyloid-beta aggregation

Session

Poster Session One

Authors

Mr Gabriel Ing (2), Dr Lorena Ruiz-Perez (1), Dr Andy Stewart (2), Prof Giuseppe Battaglia (1)

Affiliations

1. Institute for Bioengineering of Catalonia
2. University College London

Keywords

Liquid-Phase transmission electron microscopy  Amyloid-β In-situ-TEM 

Abstract text

Liquid-phase electron microscopy (LPEM) is a powerful technique to study the dynamics of molecular processes occurring in real time. While the technique is becoming increasingly established in inorganic and metal-containing systems, the next frontier of LPEM is the study of organic and biological material at the molecular level. Here I present our research imaging the peptide  amyloid-β with LPEM. Amyloid-β is a small peptide found in the brain, which aggregates to form larger structures, including fibrils and toxic oligomers, but the pathway for this process is currently unknown. The relevance of this question is paramount, as the pathway is highly associated with Alzheimer’s disease, with drug design studies attempting to alter the aggregation.  At present, we have imaged fibrils and oligomers, and also visualised what appears to be primary and secondary nucleation processes, these are key steps in the aggregation pathway. We also have evidence to suggest that liquid-liquid phase-separation of amyloid-β from solution could play a role in this process, with liquid-phase droplets being observed. We believe that amyloid-β is a perfect system for the unique strengths of LPEM to advance our knowledge of biology in new ways, demonstrating the capabilities of the method.

References