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Identification of Potential Drug Target Gives New Hope for Alzheimer's Patients
The researchers believe that the finding made in the laboratory of Michael T. Bowers, a professor of Chemistry and Biochemistry at UCSB, may lead to new drugs for the disease.
In their study report, they have explained the process in which the toxic Amyloid Beta 42 peptides aggregate, and outlined the new technology they use to study these peptides.
"We believe that we have put a face, a structure, on the molecular assembly that is responsible for Alzheimer's disease," Nature magazine quoted Bowers as saying.
He and his colleagues used an innovative technology called ion mobility-based mass spectroscopy, a method that allows researchers to investigate the structure, aggregation, and energetics of protein and peptide systems.
The Amyloid Beta (AB) 42 peptide is clipped from a much larger protein, the amyloid precursor protein (APP), and is composed of 42 amino acid residues.
A second peptide, AB40, is 10 times more abundant than AB42 in healthy human brains, and is also clipped from APP. It is identical to AB42 except it is missing the last two amino acids.
Both peptides aggregate, but AB42 more so than AB40.
Bowers points out that AB40 never grows beyond a tetramer-a cluster of four AB40 peptides. As a consequence, it is nontoxic.
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