Use of amyloid inhibitors cautioned

Brian Shoichet, PhD, School of Pharmacy faculty member and Brian Feng, PhD, former staff research associate with the School, and colleagues have discovered that many amyloid inhibitors, which scientists had hoped would keep "sticky" amyloid protein fibers such as those associated with Alzheimer's disease from aggregating in brain tissue, actually clump together themselves. This would make these amyloid inhibitors useless as targeted therapies against amyloid in the brain. In addition, in their clumped form, they inhibit most other proteins with which they come in contact. Their work appears in the January 27, 2008 issue of Nature Chemical Biology under the title "Small-molecule aggregates inhibit amyloid polymerization."

"A cautionary conclusion to emerge from these studies," write the authors, "is that chemical aggregators may be common among inhibitors of amyloid fibrillization."

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Small molecule aggregates inhibit amyloid polymerization


School of Pharmacy, Department of Pharmaceutical Chemistry, PharmD Degree Program, BMI, QBC, CCB, PSPG, Bioinformatics, Biophysics

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