Researchers at Emory University and Argonne National Laboratory have discovered a new method to manipulate the self-assembly and formation of amyloid fibrils, a major component of brain plaques associated with Alzheimer’s disease, thereby opening new avenues for examination of their formation and for the construction of robust nanotubes that have potential applications in research, industry and medicine.
Certain short amino acid chains, the building blocks of proteins, are capable of self-assembly into the disease-causing amyloid fibrils of Alzheimer’s. Emory biochemistry professor David Lynn and his colleagues have now enticed these amyloid peptides to self-assemble into well-defined nanotubes 15 billionths of a meter across. Such nanotubes can now serve as minute scaffolds to build nanotechnological devices with potential applications in many fields. These findings are published in the May 21 issue of the Journal of the American Chemical Society in their paper "Exploiting Amyloid Fibril Lamination for Nanotube Self-Assembly."
"We took what we know about amyloid fibril self-assembly, and used that information to construct novel, self-assembling nanotubes. The creation of these new structures will in turn teach us more about the physical properties of amyloids and the pathways to their formation, which puts us in a better position to understand why they are so damaging and cause disease," says Lynn.
Deb Hammacher | EurekAlert!
Novel anti-cancer nanomedicine for efficient chemotherapy
17.09.2019 | University of Helsinki
Researchers have identified areas of the retina that change in mild Alzheimer's disease
16.09.2019 | Universidad Complutense de Madrid
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.
The functions of biomolecules are determined by their motions and structural changes. Yet it is a formidable challenge to understand these dynamic motions.
At the International Symposium on Automotive Lighting 2019 (ISAL) in Darmstadt from September 23 to 25, 2019, the Fraunhofer Institute for Organic Electronics, Electron Beam and Plasma Technology FEP, a provider of research and development services in the field of organic electronics, will present OLED light strips of any length with additional functionalities for the first time at booth no. 37.
Almost everyone is familiar with light strips for interior design. LED strips are available by the metre in DIY stores around the corner and are just as often...
Later during this century, around 2060, a paradigm shift in global energy consumption is expected: we will spend more energy for cooling than for heating....
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.
If you want to build the most accurate clock in the world, you need something that "ticks" very fast and extremely precise. In an atomic clock, electrons are...
10.09.2019 | Event News
04.09.2019 | Event News
29.08.2019 | Event News
18.09.2019 | Innovative Products
18.09.2019 | Physics and Astronomy
18.09.2019 | Materials Sciences