A probe invented at Rice University that lights up when it binds to a misfolded amyloid beta peptide — the kind suspected of causing Alzheimer’s disease — has identified a specific binding site on the protein that could facilitate better drugs to treat the disease.
A probe invented at Rice University that lights up when it binds to a misfolded amyloid beta peptide — the kind suspected of causing Alzheimer’s disease — has identified a specific binding site on the protein that could facilitate better drugs to treat the disease.
Even better, the lab has discovered that when the metallic probe is illuminated, it catalyzes oxidation of the protein in a way they believe might keep it from aggregating in the brains of patients.
The study done on long amyloid fibrils backs up computer simulations by colleagues at the University of Miami that predicted the photoluminescent metal complex would attach itself to the amyloid peptide near a hydrophobic (water-avoiding) cleft that appears on the surface of the fibril aggregate. That cleft presents a new target for drugs.
Finding the site was relatively simple once the lab of Rice chemist Angel Martí used its rhenium-based complexes to target fibrils. The light-switching complex glows when hit with ultraviolet light, but when it binds to the fibril it becomes more than 100 times brighter and causes oxidation of the amyloid peptide.
Read more at Rice University
Image: From left, Rice University research scientist Christopher Pennington, graduate student Bo Jiang and Angel Martí, an associate professor of chemistry and bioengineering, run an amyloid beta experiment in the Martí lab. (Photo by Brandon Martin)
