Short biography
Natàlia received her BSc in Chemistry and a MSc in Organic Chemistry from the University of Barcelona. In 1996, she started her Ph.D. at the University of Minnesota in the laboratories of Prof. Barany and Prof. Woodward. During her Ph.D., she successfully produced and characterized the first designed water soluble four stranded ß-sheet protein. In 2001, she went on to join Prof. Dobson´s research group at Cambridge University where she worked on amyloid fibril formation, a process involved in important diseases such as Alzheimer´s and Parkinson´s. While at Cambridge, she discovered a completely novel mechanism that involves the continuous dissolution and reformation of individual amyloid fibrils, which has considerable importance for the rational design of therapeutics. In 2003, Natàlia joined the laboratory of Prof. Giralt at the IRB where she is developing and applying new approaches to characterize the structural and dynamic properties of the species involved in amyloid formation. Research interests
The origin and progression of Alzheimer´s disease (AD) has been linked to the process of amyloid-ß protein (Aß) aggregation that ultimately leads to amyloid fibrils. Aß amyloid fibril formation is a multistep process during which intermediate aggregation species are formed. Although early hypotheses proposed amyloid fibrils as the primary pathogenic cause, recent evidences support that intermediates in the fibril assembly process represent the primary culprits of these diseases. The research we carry out focuses on the study of the structure and dynamics of all the species involved in the process of Aß amyloid fibril formation. Our aim is to fully understand this process so that it can be applied to the development of treatments for AD.
Key words
Alzheimer´s disease, aggregates, amyloid fibrils, hydrogen/deuterium exchange, nuclear magnetic resonance spectroscopy, mass spectrometry