In the search for new treatment options for various diseases, a thorough understanding of the structure of related molecules is needed. Many methods are utilized in science to investigate the structure of biological molecules, and among those that give information on the smallest scale is X-ray Absorption Spectroscopy (XAS).
The current dissertation explores the possibilities and limitations of XAS when applied to biological systems. While experiments of this type is often associated with radiation damage to the samples, a way of avoiding this is explored. By the use of a flow cell, the sample is replaced continuously during measurements.
A biological molecule called amyloid-β (Aβ), associated to Alzheimer’s disease, is investigated using XAS. Aβ has been found to bind copper and zinc in the brains of patients with Alzheimer’s disease, and the specific structure around copper and zinc is presented at various conditions. Another, more well described protein called plastocyanin and the local structure around copper inside, was also investigated. The structure was found to be very similar to the consensus from other studies. However, a high level of radiation damage was also detected, sparking speculations that the consensus is established around the damaged structure