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Prof. Rahimipour's Lab

Prof. Rahimipour's Lab



Tel: 972-3-531-7412
Fax: 972-3-738-4053

Drug Discovery, Design, and Delivery Research for Neurodegenerative Diseases

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 design and discovery of novel anti-amyloidogenic compounds with potential application in different neurodegenerative diseases, such asAlzheimer’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.

Inflammatory Disease Research: Multiple Sclerosis

Rahimipour’s group is also trying to develop new therapeutics for Multiple Sclerosis (MS).

It is generally accepted that the major determinant of progressive neurological disability in MS patients is axonal degeneration and demyelination, which are due to a combination of circulating reactive oxygen species (ROS) and reactive nitrogen species (RNS), as well as imbalanced glutamate metabolism.

The assumption is that multifunctional agents that exhibit neuroprotecting and antioxidant activity are excellent drug candidates for MS. However, there are several inherent limitations on the use of most available antioxidants, as they suffer from low bioactivity and bioavailability, poor biostability and systemic toxicity.

Rahimipour’s group tries to overcome some of these drawbacks by utilizing a multivalent approach used in nature to dramatically increase the bioactivity of ligands with low individual activity.

They utilize the multivalency properties of novel self-assembled peptides to develop therapeutic agentsthat possess anti-inflammatory, anti-oxidant and anti-excitotoxic activity,and then evaluate the protective effects of these molecules on axonal damage.

Using this approach, Rahimipour’s team has recently discovered novel peptides that exhibit potent, neuroprotecting activity both in-vitro and in animal models of MS.

Infectious Disease Research

Rahimipour and his team are also developing a method whereby they can modify different surfaces such as metals, polymers, and inorganic materials with an adhesive protein mimic that acts as a “two-sided adhesive coating.”

They have shown that by covalently attaching antibacterial peptides and anti-fouling quaternary amines to the modified surfaces, these surfaces kill bacteria on contact.

Moreover, these surfaces have proven to be stable under different conditions, and the fabricated substances are not leached to the environment.  

Rahimipour’s goal is to design and construct novel antibacterial and antifouling surfaces by developing a robust and inexpensive technique that could be applied to different surfaces, reducing the spread of many infectious diseases. Such surfaces would be invaluable for a multitude of purposes.

Examples include medical applications such as implants and indwelling catheters, self-disinfecting surfaces such as textile, glass, and polymers in public environments, marine antifouling technologies, and handheld or other consumer devices such as cell phones and toys.

The main advantages of this method are its robustness and simplicity, low cost production, non-toxicity and its capability to be used to modify large surfaces.

Areas of Interest

One of the major goals of Rahimipour’s group is to better understand and utilize self-assembly processes in order to design new modalities for arresting amyloid formation, and to enhance the biological activity and multimodal activity of different pharmacophores by inducing multivalency.

Last updated on 11/8/15