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Use of amyloid inhibitors cautioned
By UCSF School of Pharmacy Editorial Staff / Thu Jan 31, 2008
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."
School of Pharmacy, Department of Pharmaceutical Chemistry, PharmD Degree Program, BMI, QBC, CCB, PSPG, Bioinformatics, Biophysics
About the School: The UCSF School of Pharmacy aims to solve the most pressing health care problems and strives to ensure that each patient receives the safest, most effective treatments. Our discoveries seed the development of novel therapies, and our researchers consistently lead the nation in NIH funding. The School’s doctor of pharmacy (PharmD) degree program, with its unique emphasis on scientific thinking, prepares students to be critical thinkers and leaders in their field.