Proteins are large molecular chains that move around cells carrying vital information on the activity of the organism. The role of each protein depends largely on the form it takes, but the proteins occasionally lose this form when they collide and bind with other proteins. They aggregate, and lose their function, growing continuously to form what are known as amyloid fibres. This causes neurodegenerative diseases, such as Parkinson’s, Alzheimer’s, and forms of spongiform encephalopathy, such as mad cow disease (BSE) and its human form, Creuzfeldt-Jacob disease. It also produces the pancreatic malfunctions that cause type 2 diabetes.
A team of scientists from the Universitat Autònoma de Barcelona, led by the researcher Salvador Ventura, has developed a method that allows those parts of the proteins that set off aggregation to be identified. Using this method one is able to identify the precise zones of each protein that force these proteins to bond, aggregate and form amyloid fibres. The scientists have tested the method with different proteins involved in conformational diseases, while identifying zones that were already known for their role in protein aggregation and the diseases mentioned above.
According to Salvador Ventura, their method “identifies potential therapeutic targets against illnesses caused by protein aggregation, such as Alzheimer’s, Parkinson’s and type 2 diabetes. It allows a more precise identification of the targets, meaning that in theory they can be attacked more effectively”.
Octavi López Coronado | alfa
Closing in on advanced prostate cancer
13.12.2017 | Institute for Research in Biomedicine (IRB Barcelona)
Visualizing single molecules in whole cells with a new spin
13.12.2017 | Wyss Institute for Biologically Inspired Engineering at Harvard
MPQ scientists achieve long storage times for photonic quantum bits which break the lower bound for direct teleportation in a global quantum network.
Concerning the development of quantum memories for the realization of global quantum networks, scientists of the Quantum Dynamics Division led by Professor...
Researchers have developed a water cloaking concept based on electromagnetic forces that could eliminate an object's wake, greatly reducing its drag while...
Tiny pores at a cell's entryway act as miniature bouncers, letting in some electrically charged atoms--ions--but blocking others. Operating as exquisitely sensitive filters, these "ion channels" play a critical role in biological functions such as muscle contraction and the firing of brain cells.
To rapidly transport the right ions through the cell membrane, the tiny channels rely on a complex interplay between the ions and surrounding molecules,...
The miniaturization of the current technology of storage media is hindered by fundamental limits of quantum mechanics. A new approach consists in using so-called spin-crossover molecules as the smallest possible storage unit. Similar to normal hard drives, these special molecules can save information via their magnetic state. A research team from Kiel University has now managed to successfully place a new class of spin-crossover molecules onto a surface and to improve the molecule’s storage capacity. The storage density of conventional hard drives could therefore theoretically be increased by more than one hundred fold. The study has been published in the scientific journal Nano Letters.
Over the past few years, the building blocks of storage media have gotten ever smaller. But further miniaturization of the current technology is hindered by...
With innovative experiments, researchers at the Helmholtz-Zentrums Geesthacht and the Technical University Hamburg unravel why tiny metallic structures are extremely strong
Light-weight and simultaneously strong – porous metallic nanomaterials promise interesting applications as, for instance, for future aeroplanes with enhanced...
11.12.2017 | Event News
08.12.2017 | Event News
07.12.2017 | Event News
13.12.2017 | Health and Medicine
13.12.2017 | Physics and Astronomy
13.12.2017 | Life Sciences