School of Biomedical Sciences cordially invites you to join the following seminar:

Speaker: Dr. Javier Oroz, Assistant Professor, Blas Cabrera Institute for Physical Chemistry, Madrid, Spain
Talk Title: Metamorphic structures priming alternative aggregates in human diseases

Date: 21 May 2025 (Wednesday)
Time: 4:00 pm – 5:00 pm
Venue: Seminar Room 3, G/F, Laboratory Block, 21 Sassoon Road
Host: Professor Rubén Hervas Millan

Biography

Dr. Oroz graduated in Biology and Biochemistry from the University of Navarra in 2004. He then moved to the Cajal Institute of Neurobiology in Madrid to carry out his Ph.D. with Mariano Carrión-Vázquez, where he applied biophysics and structural biology to understand conformational transitions in the early stages of amyloid aggregation. After earning his Ph.D. in 2010, Dr. Oroz moved as a postdoc to the CIB Institute (Madrid) to be instructed in protein NMR by Eva de Alba. In 2013, Dr. Oroz moved to the Max Planck Institute in Göttingen with Markus Zweckstetter to apply top-notch NMR methodologies to determine the structure of complexes formed by chaperones and amyloidogenic clients. Dr. Oroz moved in 2018 to the Blas Cabrera Institute for Physical Chemistry in Madrid where he has established his independent group focused on the structural biology of prionoids. Dr. Oroz is Assistant Professor since 2023. Currently he is visiting the HKU to learn state-of-the-art cryo-EM with Rubén Hervás.

Abstract

Metamorphic proteins show fast interconverting structural conformations and often trigger aberrant protein deposits. This prion-like, irreversible protein aggregation may cause cellular degeneration and is related to more than 50 human diseases. Insights on the structures priming deleterious assembly not only provide fundamental understanding on the mechanisms causing cellular toxicity, but also expedite the development of diagnostic or intervention bullets. However, although deciphering the structures of shapeshifting protein conformers is a methodological challenge, NMR spectroscopy provides unbeatable information for the mechanistic understanding of deleterious protein aggregation processes. Applying this methodology, we have managed to describe the principles for protein loss of function in several human diseases, such as amyloidosis, ALS or CCHS. I will show practical examples how these insights may open the door for the development of diagnostic tools or help for the high-throughput search of therapeutic compounds in incurable human diseases.

ALL ARE WELCOME.