Binding Sites on Amyloid Beta Peptide Discovered
by Neuroscience News
A rhenium-based complex developed at Rice University binds to fibrils of misfolded amyloid beta peptide, which marks the location of a hydrophobic cleft that could serve as a drug target, and oxidizes the fibril, which changes its chemistry in a way that could prevent further aggregation. NeuroscienceNews.com image is credited to Martà Group/Rice University.
Researchers have invented a probe that lights up when it binds to a misfolded amyloid peptide.
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