According to an unsettling, new research

Apr 8, 2010 10:11 GMT  ·  By
Protein segments with a 'steric zipper' structure mesh tightly to form the spine of amyloid fibrils
   Protein segments with a 'steric zipper' structure mesh tightly to form the spine of amyloid fibrils

The severity of diseases such as Alzheimer's and Creutzfeldt–Jakob is no longer a secret for many. The most common elements that hint the nature of the neurological affection to healthcare specialists are structures known as amyloid fibers, which are produced by a sticky substance on the surface of proteins. Eventually, other molecules accumulate, and nerve cells, for instance, become entangled, and unable to function. A new scientific research has demonstrated that virtually all complex proteins in the body can form amyloids, which is a very worrying conclusion, Nature News reports.

Basically, amyloids are nothing more than sticky aggregates that unfortunately play an important role in neurodegenerative brain disorders. What the team behind the new study found was that almost all human proteins have segments on them that can form these structures. The investigation was conducted by scientists at the University of California in Los Angeles (UCLA), led by expert David Eisenberg. He and his team found that “effectively all complex proteins have these short segments that, if exposed and flexible enough, are capable of triggering amyloid formation.” The work covered several tens of thousands of proteins, the researcher adds.

Eisenberg proposes that human evolution played a considerable role in keeping amyloids in check. He reveals that the human body appears to be locked in a never-ending struggle, each cell at a time, against the natural tendency that proteins have to form these sticky aggregates. The team leader explains that evolution appears to treat amyloids as a fundamental threat to the very survival of our species. “The amyloid state is more like the default state of a protein, and in the absence of specific protective mechanisms, many of our proteins could fall into it,” University of Cambridge structural biologist Chris Dobson says.

“Advances in understanding amyloids could lead to a powerful new class of medicines for many age-related conditions,” adds Mount Sinai School of Medicine in New York neurobiologist and clinician Sam Gandy. At this point, many research laboratories around the world are working on therapies that seek to augment the natural defense mechanisms cells employ against amyloid formation, in hopes of producing more viable courses of treatment for diseases such as Alzheimer's.