The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

NanoLund Seminar Series

This seminar series aim to increase the awareness among ourselves about all of the ongoing cutting-edge research within the different fields of nanotechnology carried out by the close to 100 research groups in NanoLund. The seminars in this series will consist of two parts. The first part (45 min) consists of a lecture followed by questions, and after five minutes break, we will continue with a 30 min session to discuss ideas and possible collaborations.

NanoLund Seminar 11 March 15:15

Oxana Klementieva Portrait

Speaker: Oxana Klementieva

Title: Combining microspectroscopy and neurobiology for understanding Alzheimer’s disease

Date and Time: Thursday, 11 March 2021 at 15.15

Zoom-linkhttps://lu-se.zoom.us/j/6889174192

Abstract:

Alzheimer's disease affects the lives of millions of people worldwide, already costing about 1 % of the global economy. Alzheimer's disease is characterized by the formation of protein amyloid aggregates, so-called amyloid oligomers. These oligomers are characterized by specific β-sheet structures and are thought to be neurotoxic. However, the secondary structure of amyloid oligomers is polymorphic and the structure that contributes most to the neurotoxicity is unknown. This lack of knowledge exists mainly because it is incredibly challenging to characterize the secondary structure of amyloid proteins directly in cells. To investigate molecular changes in proteins directly in cells, we used synchrotron-based infrared microspectroscopy, a label-free and non-destructive technique available for in situ molecular imaging. Specifically, we evaluated the formation of β-sheet structures in cells that simultaneously express amyloid β and alpha synuclein, amyloid β and Tau, models of pure and mixed amyloid aggregation related to Alzheimer's disease.