About 24 million people around the world suffer from neurodegenerative diseases similar to Alzheimers, Parkinsons, or Huntington’s. The molecular generation of these diseases has so far been little investigated. A group of scientists from Leipzig University and the Technical University of Dresden, in addition to the Kurt Schwabe Institute Meinsberg – is now looking into these molecular mechanisms with new proposals and has developed a technique involving a thermal molecule trap. The researchers have reported their findings in Nature Methods.
Researchers assume that the reason for these neurodegenerative diseases is the aggregation of small protein molecules called peptides. Peptides typically carry out completely different duties within the body with their particular three-dimensional structure. For instance, they act as hormones, and they’re concerned within the transport of substances via the cell membrane and have antibiotic and antiviral functions. Nevertheless, when peptides come together to kind small aggregates and even bigger insoluble structures referred to as plaques or amyloids, their unique role is lost, and peptide aggregates can be toxic.
The researchers have come up with new explanatory approaches: “When analyzing mixtures of single molecules, aggregates, and fibrils for their properties, one obtains an image of many overlapping effects. A vital step in the direction of an in-depth perception at the molecular level is to review the growth of individual amyloid fibrils,” explains Prof. Dr. Frank Cichos, head of the project at Leipzig University.
Utilizing their newly developed thermal trap, the researchers trapped individual fibrils in physiological options for several hours beneath the microscope and for the first time, noticed the growth of the fibril, its breakup and the additional growth of the fragments. Developing a technique for this purpose was a tricky task. Molecules in liquids move steadily because of the temperature of the liquid. This so-known as Brownian movement shortly drives them out of our field of observation, and we can solely observe individual fibrils for a short time, says Martin Fränzl, a doctoral candidate in the project.