The first three-dimensional picture of the amyloid deposits in the brains of Alzheimer's patients has been mapped by a team of American and German researchers.
The research team-comprising of experts from Brandeis University in Waltham, Massachusetts and the Leibniz Institut in Jena, Germany-claims to be the first to show how A-beta peptide forms a spaghetti-like protein mass called an amyloid fibril.
The study, appearing in the Proceedings of the National Academy of Sciences, is being considered to be a big leap towards understanding the role such protein clumps play in the development of neurodegenerative disease.
"This study is a significant advance regarding our understanding of how these fibrils are built from the A-beta peptide (Alzheimer's peptide)," said co-author Nikolaus Grigorieff, a biophysicist at Brandeis University and an investigator with the Howard Hughes Medical Institute.
"People have been guessing for decades what these fibrils look like, but now we have an actual 3D image," he added.
Grigorieff says that he wants to identify which part of the amyloid structure is toxic, as that would be an important step in designing drugs to prevent or treat disease.
He revealed that the image produced with the help of electron microscopy showed how the peptide, a series of linked amino acids, was arranged in the tape-like fibril.
"The next step will be a 3-D image that tells us exactly where all the amino acids are. This will tell us more about the chemical and biological properties of A-beta fibrils that we need to know to understand their role in Alzheimer's," said Grigorieff.