Shai Rahimipour, Ph.D.
Senior Lecturer, Department of Chemistry - Bar-Ilan University (Israel)
Surface-Modified Proteinous Microspheres and Self-assembled Cyclic D,L-alpha-Peptides as Potential Therapeutics for Alzheimer's Diseases
Protein misfolding and aggregation is the fundamental cause of many amyloidogenic diseases. The deposition of proteins in the form of amyloid fibrils and plaques is the characteristic feature of more than 20 degenerative conditions affecting either the central nervous system or a variety of peripheral tissues. For Alzheimer's disease (AD), the oligomerization of amyloid beta (Aß) to soluble oligomers and their accumulation in the brain are believed to be the primary pathogenic events that lead to synaptic loss and selective neuronal cell death. Therefore, reducing Aß levels in the brain by recruiting the immune system or inhibiting Aß aggregation via agents that interfere with its self-assembly are promising strategies for AD therapy. In this presentation, I will describe our recent efforts in developing surface-modified proteinous microspheres that can selectively bind Aß, enhance its clearance by macrophages and reduce its toxicity. I will also describe the development of novel self-assembled cyclic D,L-a-peptide nano-architectures that interact strongly with A and inhibit its aggregation and toxicity due to their immense structural-functional similarities to that of different amyloids. The in vitro and mechanistic studies of these kinds of peptide architectures will be also discussed.
Date of update July 3, 2013