?Cap blocking the molecular processes leading to Alzheimer's ...

Amyloid fibers are elongated, water-resistant structures consisting of two sheets of related proteins. The proteins of each sheet to contribute side chains, causing them to interlock like the teeth of a zipper, Eisenberg said.The results were spectacular. The introduction of an inhibitor of tau protein solution completely prevented the formation of amyloid fibers, supporting the idea that the design of the structure-based treatments for disease amyloid is a viable option.

Inhibitors of tau and SEVI were designed as synthetic amino acids, similar to proteins in the body of standard bricks. But these synthetic amino acids have been returned, as if seen through a glass, or had added side chains are not normally found in nature. The enzymes in the human body that are programmed to break the chains of proteins, as they are, in principle, able to recognize unnatural amino acids, keeping blockers safe to hang on the target proteins.

The fibers are not only Alzheimer?s disease, but in a variety of conditions, including type II and a family of disorders related to mad cow disease, among others. In Alzheimer?s disease and other neurodegenerative diseases, tau protein forms amyloid fibers inside of brain cells, destroying them through a mechanism that is still under investigation.

A research team led by second Eisenberg has recently announced that it has identified four small molecules that bind to amyloid fibers, including a promising candidate called ?orange-G? gets stuck in the hinge, such as fiber and may be able to break.

?By studying the structures of two key proteins that form amyloid, we were able to identify the small chain of amino acids responsible for the formation of amyloid fibers and engineering a? molecular cap ?that attaches the fiber ends to inhibit their growth ?said leading research David Eisenberg, director of the UCLA-DOE Institute of Genomics and Proteomics and Howard Hughes Medical Institute.

Co-authors of this research include UCLA Kym Faull, Professor of Psychiatry and Biobehavioral Sciences, Jorge Barrio, a professor of molecular pharmacology and medical researchers Michael Sawaya and Jie Liu, postdoctoral researchers Meytal Landau, Lin Jiang and Stuart Sievers, and graduate student Arthur Laganowsky.

Eisenberg and his research team has discovered that all the tau proteins, a small chain of only six amino acids ? in short VQIVYK ? was responsible for the formation of amyloid fibers. By studying the structure of the fibers using microcrystallography, a method developed at UCLA for this research, the team was able to use the fiber as a model for designing an inhibitor that ?cap? of the fiber and continue to grow.

This study was published June 14 PLoS Biology, an online journal Public Library of Science.

Other co-authors of the study included postdoctoral scholars at UCLA Stuart Sievers and Lin Jiang, UCLA graduate students and Anni Howard Chang Zhao, John Karanicolas, an assistant professor at the University of Kansas, Jason Stevens, a series of University of Kansas, David Baker, a professor at the University of Washington, and Professor Jan M nch Zirafi Onofrio and researcher at the University of Ulm in Germany.

Although tau and SEVI have different structures and other features that form amyloid fibers with a similar morphology, which makes it possible to design two separate inhibitors using the same process, according to Eisenberg.

?Even if the tests are many, it seems that we might be on the way to develop a therapy,? said Eisenberg. ?Our hope is that we could do a blocker that could be applied with a vaginal gel or spray that may help prevent HIV infection.?

Newly developed by biochemists at UCLA has brought scientists closer to developing treatments that could delay the onset and prevention of sexual transmission.

This research was federally funded by the National Institutes of Health, the National Science Foundation and the U. S. Department of Energy and the Howard Hughes Medical Institute and the Joint Centre for translational medicine.

The study was published online June 15 in the journal Nature and will be available in a print edition to come.

?These are displayed as the first small molecules bind to amyloid-like fibers,? said Eisenberg. ?These small molecules are less likely to be broken in the body and can be modified to force the exception of the amyloid fibers or serve as diagnostic tools to identify the infected areas of the body.?

Despite this success, there is still a long way to do it for a living can be developed to combat the onset of Alzheimer?s disease in human patients, said Eisenberg. The inhibitor, a chain of amino acids, is too large to penetrate deep into the brain, where tau proteins form amyloid fibers.

?This research is an important step towards the identification of small molecules that can be used to develop a therapy,? said Eisenberg. ?Our goal is to be able to delay the onset of Alzheimer?s disease.?

?The care of many patients with this debilitating disease could be a significant fraction of the U.S. gross domestic product.?

?The presence of SEVI makes the rate of HIV infection through sexual contact up to 100,000 times more at risk,? he said. ?Block SEVI, we have a method to inhibit the sexual transmission of HIV.?

?In 10 years we got to the point where we begin to understand the structural biology of amyloid fibers and how to inhibit them and how to interfere with them,? said Eisenberg.

?The next step is to make molecules that inhibit the practice and break the amyloid fibers ? which is the ultimate goal.?

Source: http://www.exercise24.org/?p=234

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