Professor David Eisenberg, University of California in Los Angeles, USA, has been awarded the Gregori Aminoff Prize in Crystallography by the Royal Swedish Academy of Sciences. He has pioneered the study of amyloid proteins’ molecular structure, providing new knowledge about neurodegenerative diseases such as Parkinson’s. This may benefit the development of new pharmaceuticals.
The crystals are smaller than the wavelength of light and are, in principle, impossible to handle – they are so small that they cannot be mounted in standard X-ray equipment. To overcome this, David Eisenberg located the crystals using an electron microscope and performed electron diffraction. This meant that their structures could be solved at a very high resolution.
One early example was part of the α-synuclein protein from Parkinson’s disease. He directed an extremely weak electron beam at the nanocrystals in the electron microscope, obtaining a diffraction pattern that allowed structure determination. Recently, he has also used cryo-electron microscopy, in which fibrils and fibril-inhibitor complexes are frozen. This allows their structures to be determined and also reveals co-existing structures and their populations.
Can damage nerve cells in the brain
In neurodegenerative diseases, amyloid fibrils form. These needle-shaped aggregates are made from what are usually functional proteins in the brain. They can lead to organ failure, or intermediate forms of the proteins can damage nerve cells. Important questions to explore in this area are how they transform into fibrils, as well as identifying which forms are toxic. Here, knowledge of their structures in these diseases is vital.
“…has pushed the frontiers”
David Eisenberg is a pioneering researcher in the field of protein structural biology. His early work concerned folded proteins and a phenomenon called domain swapping. However, in recent decades, he has led the determination of high-resolution structural models of amyloid fibrils. His research has a strong emphasis on method development, and methodology in structural biology is evolving over time.
“David Eisenberg has worked incredibly hard and has pushed the frontiers of this challenging field. One groundbreaking achievement was the formation of micrometre-sized crystals of short peptides in fibril form, then believed to be impossible, and the determination of their structures using X-ray crystallography,” says Sara Snogerup Linse, member of the Royal Swedish Academy of Sciences.
Citation
“For his discoveries of amyloid fibril structures of relevance for the field of amyloid structural biology and neurodegenerative diseases”.
About the Laureate
David Eisenberg is Professor of Chemistry and Biochemistry and Biological Chemistry at UCLA (University of California Los Angeles) and a Howard Hughes Medical Institute Investigator. He received his DPhil in theoretical chemistry from the University of Oxford in 1965 and then worked at Princeton and Caltech before moving to UCLA in the early 1970s.
About the Gregori Aminoff Prize
Every year, the Gregori Aminoff Prize in crystallography is awarded by the Royal Swedish Academy of Sciences. The Prize recognises a documented individual contribution to the field of crystallography and has been awarded to Swedish and foreign researchers since 1979. The prize money is 150,000 Swedish kronor. Crystallography is the study of atomic structures in solid materials and is used in chemistry, biology, medicine, geology and materials science.
Contact
Expert
Sara Snogerup Linse
Professor of Physical Chemistry at Lund University
sara.linse@biochemistry.lu.se
Press contact
Eva Nevelius, pressansvarig vid Vetenskapsakademien
eva.nevelius@kva.se
070-878 67 63
