Neuro-Chemistry of Neurodegenerative Diseases
Our team works on neurodegenerative diseases, such as Alzheimer's and Huntington's disease by using several animal models, cells, and human tissues. We synthesize and modify peptides that help to diagnose Alzheimer's and provide therapy
Rahimipour Lab
Research
Prof. Shai Rahimipour is a returning scientist from the Scripps Research Institute in California and an Associate Prof. in BIU’s Department of Chemistry.
Rahimipour and his team are trying to develop a molecular-based platform that can be used as a general scaffold for designing and discovering novel anti-amyloidogenic compounds with potential applications in different neurodegenerative diseases, such as Alzheimer’s disease (AD).
Towards this goal, the group has rationally designed and synthesized novel cyclic peptides that can bind pathogenic amyloid beta protein (Ab) accumulated in the brains of AD patients, thus reducing its aggregation and preventing neurotoxicity.
Moreover, these peptides were found to dissolve pre-formed protein fibers. In another project, they have designed and constructed proteinaceous particles that exhibit multimodal activity, blocking amyloid aggregation and stimulating the body’s immune system to clear Ab.
My group seeks to develop a supramolecular-based platform that can be used as a general scaffold for the design and discovery of novel anti-amyloidogenic compounds with potential application in the treatment of various amyloidogenic diseases, such as Alzheimer’s disease, Parkinson’s disease and type II diabetes. Recent biochemical and biophysical studies have shown that pathogenic amyloids share standard structural and functional features despite being composed of different proteins and amino acids. The similarities between the different amyloids are so immense that soluble aggregates of diverse amyloidogenic proteins, such as insulin, islet amyloid polypeptide, and a-synuclein, can cross-react with each other and be equally recognized by polyclonal antibodies raised against prefibrillar assemblies of amyloid b (Ab) peptides, which are responsible for Alzheimer’s disease. Astonishingly, we have recently found great structural and functional similarities between Ab and the self-assembled cyclic D,L-a-peptides, which lead the latter to cross-react with Ab and modulate its aggregation and toxicity. Moreover, we have shown that the self-assembled cyclic D,L-a-peptides may interact also with other pathogenic amyloids, such as a-Syn and insulin, and inhibit their aggregation and toxicity too. We believe that these studies may shed light on the etiology of misfolded proteins and provide additional insights that can be used to tackle poorly understood topics in the field of misfolded protein diseases, such as the infectious nature of the amyloids and their ability to spread from cell-to-cell. These insights may eventually unravel how proteins begin to misfold to form toxic intermediates and enhance our ability to intervene in such processes.