Dr Mason explains: ‘In neurodegenerative diseases such as Alzheimer's or Parkinson's, aggregation (or clumping) of proteins into toxic fibrils (or chains) is considered to be the key pathogenic event.
However, no therapeutic agents currently exist to control this process. In particular, two proteins known as ß-amyloid and a-synuclein aggregate into fibrils, forming amyloid plaques and Lewy bodies that are characteristic of these diseases. A problem arises, however, in antagonist development; in recent years it has become established that small soluble (protofibrillar) forms of amyloid are the neurotoxic species, and that larger fibrils rather serve as reservoirs for these smaller protofibrils.’
‘Unfortunately, peptides and drugs designed to prevent amyloid have until recently been concerned with removing these larger fibrillar deposits. If compounds designed to breakdown amyloid are only partially effective then the balance will be shifted in the direction of smaller protofibrillar forms, rendering the amyloid more toxic in the process. We will use our expertise in the amyloid, protein-protein interaction, and library screening and design fields to combat this.’
This grant application follows on from Dr Mason's previous experience in the field. There are currently 700,000 people living with dementia in the UK, this will rise to more than a million in less than 20 years. At present, dementia costs the UK around £17 billion each year. Development of drugs capable of slowing or stopping the onset of Alzheimer’s or Parkinson's disease would improve the lives of millions of sufferers worldwide.
Victoria Bartholomew | alfa
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Hamburg and the European Molecular Biology Laboratory (EMBL) outstation in the city have developed a new method to watch biomolecules at work. This method dramatically simplifies starting enzymatic reactions by mixing a cocktail of small amounts of liquids with protein crystals. Determination of the protein structures at different times after mixing can be assembled into a time-lapse sequence that shows the molecular foundations of biology.
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Potsdam (both in Germany) and the University of Toronto (Canada) have pieced together a detailed time-lapse movie revealing all the major steps during the catalytic cycle of an enzyme. Surprisingly, the communication between the protein units is accomplished via a water-network akin to a string telephone. This communication is aligned with a ‘breathing’ motion, that is the expansion and contraction of the protein.
This time-lapse sequence of structures reveals dynamic motions as a fundamental element in the molecular foundations of biology.
Two research teams have succeeded simultaneously in measuring the long-sought Thorium nuclear transition, which enables extremely precise nuclear clocks. TU Wien (Vienna) is part of both teams.
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