Prof. Shai Rahimipour

Prof.
Prof. Shai Rahimipour
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CV

Education

1990 - 1993   B.Sc., Chemistry - Bar-Ilan University, Ramat-Gan, Israel

 

1993 - 2001   M.Sc./ Ph.D. (combined), Organic Chemistry and Neurobiology, The Weizmann Institute of Science, Rehovot, Israel. Subject: Potential Cytotoxic Derivatives of Gonadotropin-Releasing Hormone (GnRH): Synthesis and Biological Evaluation. Supervisors: Prof. Mati Fridkin and Yitzhak Koch, Department of Organic Chemistry and Neurobiology.

 

2001 – 2003   Post-Doctoral Research Fellow, Chemistry and Photobiology, The Weizmann Institute of Science, Rehovot, Israel. Subject: Design, synthesis and biological evaluation of Hypericin and its analogs as potential agents for photodynamic therapy (PDT). Supervisor: Prof. Yehuda, Mazur

 

2003 - 2006    Post-Doctoral Research Fellow, Chemistry, The Scripps Research Institute, La Jolla, California. Subject: Self-assembled cyclic D,L-a-peptide and cyclic D,L-a-glycopeptides nanotubes as antibacterial and anticancer agents. Supervisor: Prof. M. Reza Ghadiri

 

Positions

2006 - 2014     Senior Lecturer, Department of Chemistry, Bar-Ilan University.

 

2014 - Present   Associate Professor, Department of Chemistry, Bar-Ilan University.

 

Other professional activities

2007 - present   Member in editorial board of ARKIVOC Journal.

 

2007 - 2008       Organizing Committee of the 6th Medicinal Chemistry Conference, The Weizmann Inst. of Science.

 

2014                  Organizing Committee ofFunctional Peptide and Protein Nanostructures, May 25th -28th, 2014, Tzuba Hotel, Kibbutz Tzuba, Israel

 

Awards and fellowships

 

2003-2006       Human Frontier Science Program (HFSP) long-term fellowship for postdoctoral research.

 

2003-2004       Fulbright Postdoctoral fellowship

 

June 2000       CaP CURE award for proposed research on new drug discovery.

 

July 1999         ESCOM Awards for most outstanding poster relevant to drug discovery.

Publications

 

  1. Eckshtain-Levi M., Lavi R., Yufit D.S., Daniel B., Green O., Fleker O., Richman M., Rahimipour S., Gruzman A., Benisvy L. A versatile water-soluble chelating and radical scavenging platform. Chem. Commun. 2016, 52,2350-2353.
  2. Yeroslavsky G., Lavi R., Alishaev A., Rahimipour S. Sonochemically-produced metal-containing polydopamine nanoparticles and their antibacterial and antibiofilm activity. Langmuir. 2016, 32, 5201-5012.
  3. Chemerovski-Glikman M., Rozentur-Shkop E., Richman M., Grupi A., Getler A., Cohen H.Y., Shaked H., Wallin C., Wärmländer S.K., Haas E., Gräslund A., Chill J.H., Rahimipour S. Self-assembled cyclic D,L-α-peptides as generic conformational inhibitors of the α-synuclein aggregation and toxicity: in vitro and mechanistic studies. Chem. Eur. J. 2016, 22, 14236-14246.
  4. Tiiman A., Luo J., Wallin C., Olsson L., Lindgren J., Jarvet J., Per R., Sholts S.B., Rahimipour S., Abrahams J.P., Karlström A.E., Gräslund A., Wärmländer S.K. Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species. J. Alzheimers Dis. 2016, 54, 971-982.
  5. Frenkel-Pinter, M., Richman, M., Belostozky, A., Abu-Mokh, A., Gazit, E., Rahimipour, S.*, Segal, D.* Selective inhibition of aggregation and toxicity of a Tau-derived peptide using its glycosylated analogs. Chem. Eur. J. 2016, 22, 5945-5952 (Cover).
  6. Rahamim, G., Chemerovski-Glikman, M., Rahimipour, S. Amir, D., Haas,E. Resolution of two sub-populations of conformers and their individual dynamics by time resolved ensemble level FRET measurements. 2015, PLoS One. 2015, 10, e0143732.Schaffer, M., Bril, R., Batash, R., Ehernberg, B., Leshem, G., Rahimipour S., Shaked, Y. Screening for the radiosensitizing therapeutic activity of hypericin and its derivatives by testing tumor initiating cell viability. Clin. Cancer Drugs, 2015, 2, 119-127
  7. Ayasolla, K. R., Rai, P., Rahimipour, S., Hussain, M., Malhotra, A., Singhal, P.C. Tubular cell phenotype in HIV-associated nephropathy: role of phospholipid lysophosphatidic acid. Exp. Mol. Pathol. 2015, 99, 109-115.
  8. Chemerovski-Glikman, M., Richman, M., Rahimipour, S. New perspectives in reducing amyloid aggregation and toxicity. Isr. J. Chem. 2015, 55, 735-748.
  9. Yeroslavsky, G., Foster-Frey, J., Donovan, D. M., Rahimipour, S. Antibacterial and anti-biofilm surfaces through polydopamine-assisted immobilization of Lysostaphin as an antibacterial enzyme. Langmuir 2015, 31, 1064–1073. PDF Link
  10. Chemerovski, M., Belostozky, A., Richman M., Rahimipour, S. Structure-Based Study of Antiamyloidogenic Cyclic D,L-α-Peptides. Tetrahedron, 2014, 70, 7639-7644. PDF Link
  11. Shapira, R., Rudnick, S., Daniel, B., Viskind, O., Aisha, V., Richman, M., Perelman, A., Chill, J. H., Gruzman, A., Rahimipour, S. Multifunctional cyclic D,L-α-peptide architectures stimulate non-insulin dependent glucose uptake in skeletal muscle cells and protect them against oxidative stress, J. Med. Chem. 2013, 56, 6709-6718. PDF Link
  12. Yeroslavsky, G., Richman, M., Dawidowicz, L. O., Rahimipour S. Sonochemically produced polydopamine nanocapsules with selective antimicrobial activity. Chem Commun. 2013, 49, 5721-5723. PDF Link
  13. Richman, M., Wilik, S., Chemerovski, M., Wärmländer, S., Wahlström, A., Gräslund, A., Rahimipour, S. In Vitro and Mechanistic Studies of an Antiamyloidogenic Self- Assembled Cyclic D,L‐a-Peptide Architecture. J. Am. Chem. Soc. 2013,135, 3474-3484. PDF Link
  14. Richman, M., Perelman, A., Gertler A., Rahimipour, S. Effective Targeting of Aβ to Macrophages by Sonochemically Prepared Surface-Modified Protein Microspheres, Biomacromolecules 2013, 14, 110-116. PDF Link
  15. Baram-Pinto, D., Shukla, S., Richman, M., Gedanken, A., Rahimipour, S., Sarid, R. Surface-modified protein microspheres as potential antiviral agents. Chem. Commun. 2012, 48, 8359-8361. PDF Link  (Corresponding Authors).
  16. Shalev, T., Gopin, A., Bauer, M., Stark, R.W., Rahimipour, S., Non-leaching antimicrobial surfaces through polydopamine bio-inspired coating of quaternary ammonium salts or an ultrashort antimicrobial lipopeptide. J. Mater. Chem. 2012, 22, 2026-2032. PDF Link
  17. Richman, M., Wilk, S., Skirtenko, N., Perelman, A., Rahimipour, S., Surface-Modified Protein Microspheres Capture Amyloid-β and Inhibit its Aggregation and Toxicity. Chem. Eur. J. 2011, 17, 11171-11177. PDF Link (Cover)
  18. Skirtenko, N. Richman, M., Nitzan, Y. Gedanken, A. Rahimipour, S. A facile one-pot sonochemical synthesis of surface-coated mannosyl protein microspheres for detection and killing of bacteria. Chem. Commun. 2011, 47, 12277-12279. PDF Link (Cover).
  19. Skirtenko, N.; Tzanov, T.; Gedanken, A.; Rahimipour, S., One-Step Preparation of Multifunctional Chitosan Microspheres by a Simple Sonochemical Method. Chem. Eur. J. 2010, 16, 562-567. PDF Link
  20. Rahimipour, S.; Gescheidt, G.; Bilkis, I.; Fridkin, M.; Weiner, L., Towards the Efficiency of Pharmacologically Active Quinoid Compounds: Electron Transfer and Formation of Reactive Oxygen Species. Appl. Magn. Reson. 2010, 37, 629-648.  PDF Link
  21. Motiei, L., Rahimipour, S., Thayer, D. A., Wong, C. H., Ghadiri, M. R., Antibacterial cyclic D,L-alpha-glycopeptides. Chem. Comm. 2009, 3693-3695. .PDF Link
  22. Nicolaou, K. C., Zak, M., Rahimipour, S., Estrada, A. A., Hyup Lee, S., O’Brate, A., Giannakakou, P., Ghadiri, M. R. Discovery of a Biologically Active Thiostrepton Fragment. J. Am. Chem. Soc. (Communication), 2005, 127, 15042-4. Highlighted by Chemical & Engineering News, 2005
  23. Fridkin, G., Rahimipour, S., Ben-Aroya, N., Kapitkovsky, A., Di-Segni, S., Rosenberg, M., Kustanovich, I., Koch, Y., Gilon, C., Fridkin, M. Novel cyclic azo-bridged analogs of gonadotropin-releasing hormone. J. Pept. Sci. 2006, 12,106-115. PDF Link
  24. Rahimipour, S., Litichever-Coslovsky, N., Alaluf, M., Freeman, D., Ehrenberg, B., Weiner, L., Mazur, Y., Fridkin, M., Koch, Y.  Novel methyl helianthrones as photosensitizers: synthesis and biological evaluation. Photochem. Photobiol. 2005, 81, 250-8.
  25. Di-Segni, S. Giordano, C., Rahimipour, S., Ben-Aroya, N., Koch, Y., Fridkin, M. -sulfonamido gonadotropin-releasing hormone analogs.  Synthesis and evaluation of several parent hormone properties. J. Pept. Sci., 2005, 11, 45-52.
  26. Rahimipour, S., Ben-Aroya, N., Ziv, K., Chen, A., Fridkin, M., Koch, Y. Receptor-mediated targeting of a photosensitizer by its conjugation to gonadotropin-releasing hormone analogues. J. Med. Chem. 2003, 46, 3965-74.
  27. Rahimipour, S., Palivan, C., Barbosa, F., Bilkis, I., Koch, Y., Weiner, L., Fridkin, M., Mazur, Y., Gescheidt, G.  Chemical and photochemical electron transfer of new helianthrone derivatives: Aspects of their photodynamic activity. J. Am. Chem. Soc. 2003, 125, 1376-84.
  28. Chen, A., Ganor, Y., Rahimipour, S., Ben-Aroya, N., Koch, Y. Levite, M.  The neuropeptides GnRH-II and GnRH-I are produced by human T cells and trigger laminin receptor gene expression, adhesion, chemotaxis and homing to specific organs. Nature Med. 2002, 8, 1421-6.
  29. Chen, A., Kaganovsky, E., Rahimipour, S., Ben-Aroya, N., Okon, E., and Koch, Y. Two forms of GnRH are expressed in human breast tissue and over-expressed in breast cancer: a putative mechanism for the antiproliferative effect of GnRH by down regulation of acidic ribosomal phosphoproteins P1 and P2. Cancer Res. 2002, 62, 1036-44.
  30. Rahimipour S., Ben-Aroya N., Fridkin M. and Koch Y. Design, synthesis and evaluation of a long-acting, potent analog of gondotropin-releasing hormone. J. Med. Chem. 2001, 44, 3645-52.
  31. Chen A., Yahalom D., Laskar-Levy O., Rahimipour S., Ben-Aroya N., Koch Y., Two isoforms of gonadotropin-releasing hormone are coexpressed in neuronal cell lines. Endocrinology 2001, 142, 830-7.
  32. Braverman, S., Zafrani, Y., Rahimipour, S., Base catalyzed [2,3]-sigmatropic rearrangements of propargylic sulfonium and selenonium salts. Tetrahedron Lett. 2001, 42, 2911-4.
  33. Rahimipour S., Palivan C., Freeman D., Barbosa F., Weiner L., Mazur Y., Fridkin M. and Gescheidt G. Hypericin Derivatives: Substituent effects on radical anion formation. Photochem. Photobiol. 2001, 74, 149-56.
  34. Rahimipour S., Bilkis I., Péron V., Gescheidt G., Barbosa F., Mazur Y., Koch Y., Fridkin M., Weiner L. Generation of free radicals by emodic acid and its [D-Lys6]GnRH-conjugate. Photochem. Photobiol. 2001, 74, 226-36.
  35. Sack, I., Balazs, Y.S., Rahimipour, S., Vega, S. Peptide torsion angle measurements: Effects of non-dilute spin-pairs on carbon-observed, deuterium-dephased PM5-REDOR. J. Magn. Reson. 2001, 148, 104-14.
  36. Sack, I., Balazs, Y.S., Rahimipour, S., Vega, S. Solid-state NMR determination of peptide torsion angles: Application of 2H-dephased REDOR. J. Am. Chem. Soc., 2000, 122, 12263-69.
  37. Yahalom D., Rahimipour S., Koch Y., Ben-Aroya N., and Fridkin M. Design and synthesis of potent hexapeptide and heptapeptide gonadotropin-releasing hormone antagonists by truncation of a decapeptide analogue sequence. J. Med. Chem. 2000, 43, 2831-6.
  38. Yahalom D., Rahimipour S., Koch Y., Ben-Aroya N., and Fridkin M. Structure-activity studies of reduced-size gonadotropin-releasing hormone agonists derived from the sequence of an endothelin antagonist. J. Med. Chem. 2000, 43, 2824-30.
  39. Yahalom, D., Chen, A., Ben-Aroya, N., Rahimipour, S., Kaganovsky, E., Okon, E., Fridkin, M., Koch, Y., The gonadotropin-releasing hormone family of neuropeptides in the brain of human, bovain and rat: identification of third isoform. FEBS Lett. 1999, 463(3), 289-94.
  40. Rahimipour, S., Weiner, L., Shrestha-Dawadi, P. B., Bittner, S., Koch, Y., Fridkin, M., Cytotoxic peptides: Naphthoquinonyl derivatives of luteinizing hormone-releasing hormone. Lett. Pept. Sci. 1998, 5, 421-7.
  41. Shreshta-Dawadi, P. B., Bittner, S., Fridkin, M., Rahimipour, S., On the synthesis of naphthoquinonyl heterocyclic amino acids. Synthesis, 1996, 12, 1468-72.
  42. Rahimipour, S., Weiner, L., Fridkin, M., Shrestha-Dawadi, P. B., Bittner, S., Novel naphthoquinonyl derivatives: potential structural components for the synthesis of cytotoxic peptides. Lett. Pept. Sci. 1996, 3, 263-74.

Courses

Biochemistry (I and II)

Organic chemistry laboratory

Seminars in Bio-Organic Chemistry

Seminars in Organic Chemistry

Research

One of the major goals of my group is to better understand and treat disorders that are linked to aberrant protein folding and assembly. Our research strategy is interdisciplinary, aiming at utilizing self-assembly processes to design new modalities for arresting amyloid formation in different diseases. We also use self-assembly processes to enhance biological activity by inducing multivalency. The main thrust of my group’s research is summarized below.

Drug Discovery, Design, and Delivery Research for Amyloidogenic Diseases. 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. Very recent biochemical and biophysical studies have shown that pathogenic amyloids share common 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 that there are 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 the mechanism by which proteins begin to misfold to form toxic intermediates, and enhance our ability to intervene in such processes.

 

Frenkel-Pinter, M., Richman, M., Belostozky, A., Abu-Mokh, A., Gazit, E., Rahimipour, S.*, Segal, D.* Selective inhibition of aggregation and toxicity of a Tau-derived peptide using its glycosylated analogs. Chem. Eur. J. 2016, 22, 5945-5952 (Cover).

Tiiman A., Luo J., Wallin C., Olsson L., Lindgren J., Jarvet J., Per R., Sholts S.B., Rahimipour S., Abrahams J.P., Karlström A.E., Gräslund A., Wärmländer S.K. Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species. J. Alzheimers Dis. 2016, 54, 971-982.

Chemerovski-Glikman M., Rozentur-Shkop E., Richman M., Grupi A., Getler A., Cohen H.Y., Shaked H., Wallin C., Wärmländer S.K., Haas E., Gräslund A., Chill J.H., Rahimipour S. Self-assembled cyclic D,L-α-peptides as generic conformational inhibitors of the α-synuclein aggregation and toxicity: in vitro and mechanistic studies. Chem. Eur. J. 2016, 22, 14236-14246.

Wilik, S., Richman, M., Chemerovski, M., Wärmländer, S., Wahlström, A., Gräslund, A., Rahimipour, S. Anti-amyloidogenic self-assembled cyclic D,L-α-peptides: In vitro and mechanistic studies. J. Am. Chem. Soc. 2013,135, 3474-3484.

Chemerovski, M., Belostozky, A., Richman M., Rahimipour, S. Structure-Based Study of Antiamyloidogenic Cyclic D,L-α-Peptides. Tetrahedron, 2014, 70, 7639-7644.

Chemerovski-Glikman, M., Richman, M., Rahimipour, S. New Perspectives in Reducing Amyloid Aggregation and Toxicity. Isr. J. Chem. In Press.

 

Developing New Chemical Methods to Induce Multivalency – Application in the Field of Amyloidogenic Diseases Research. My group is also involved in developing new chemical methods to induce a multivalency effect, which is frequently used by nature to dramatically increase the bioactivity of ligands with low individual activity. These methods include the development of a new and straightforward sonochemical method to generate nano- and micro-sized particles bearing multiple copies of a bioactive elements covalently attached to their surface. We have used this technology to show that particles expressing multiple copies of the peptide KLVFF can strongly bind Ab, inhibit its aggregation, and reduce its cytotoxicity. We also found that the anti-amyloidogenic activity of these particles is significantly higher than that of an equimolar concentration of soluble KLVFF—most probably because of the multivalent presentation of the KLVFF peptide. We also showed that such surface-modified nanoparticles can dramatically reduce the inflammation associated with Ab. Initial in vivo toxicity experiments on mice and rats suggest that the particles are biocompatible even after intravenous injection of large doses. Bio-distribution and pharmacokinetic studies are now in progress.

 

Richman, M., Wilk, S., Skirtenko, N., Perelman, A., Rahimipour, S. Surface-Modified Protein Microspheres Capture Amyloid-β and Inhibit its Aggregation and Toxicity. Chem. Eur. J. 2011, 17, 11171-11177 (Cover)

Richman, M., Perelman, A., Gertler A., Rahimipour, S. Effective Targeting of Aβ to Macrophages by Sonochemically Prepared Surface-Modified Protein Microspheres, Biomacromolecules 2013, 14, 110-116.

Richman M. and Rahimipour S. Surface modified proteinaceous spherical particles and uses thereof, PCT/IB2012/054037

 

Utilizing Multivalency in the Field of Infectious Disease Research. We also used the multivalency effect induced by surface-modified particles to develop new modalities against bacterial and viral infections. In one example, we showed that the multivalent presentation of mannose on the surface of protein particles can cause bacteria that express mannose-binding receptors to tightly bind to the surface of the particles and inducing agglutination, which was used to detect (sense) low number of bacteria in solution. Moreover, we showed that loading the particles with the common antibacterial drug tetracycline significantly enhanced the antibacterial activity of the encapsulated drug. Enhanced drug activity was also observed when the surface of the particles was modified to express multiple copies of mercaptoethane sulfonate to inhibit HSV-1 infection.

Skirtenko, N. Richman, M., Nitzan, Y. Gedanken, A. Rahimipour, S. A facile one-pot sonochemical synthesis of surface-coated mannosyl protein microspheres for detection and killing of bacteria. Chem. Commun. 2011, 47, 12277-12279 (Cover).

Baram-Pinto, D., Shukla, S., Richman, M., Gedanken, A., Rahimipour, S.*, Sarid, R*. Surface-modified protein microspheres as potential antiviral agents. Chem. Commun. 2012, 48, 8359-8361.

 

Exploring another direction, we utilized mussel adhesive protein mimics (polydopamine) to modify different surfaces with a two-sided adhesive coating. The modified surfaces were then subjected to nucleophilic reactions with various substances to induce different functionalities on the surface. Using this technology, we recently succeeded in covalently modifying a wide variety of substrates (including glass, metals and polymers (polystyrene and polypropylene)) with different antibacterial and anti-fouling agents (including antimicrobial peptides, quaternary amines, and antibacterial enzymes). We demonstrated that the modified surfaces could effectively kill bacteria on contact without leaching of the active substances from these surfaces. Such surfaces are invaluable for a multitude of purposes, including reducing the spread of many infectious diseases. 

By combining the above polydopamine chemistry and sonochemistry, my team also succeeded in generating polydopamine nanoparticles that preserve all the characteristics of polydopamine. We utilized the reactivity of the nanoparticles toward different nucleophiles to introduce new functionalities onto the particles’ surfaces. More interestingly, we showed for the first time that the presence of Cu or Ag ions during sonochemical irradiation generates particles that exhibit potent antibacterial and antifouling activity, without inducing any toxicity to mammalian cells. These particles could potentially be painted onto a wide range of surfaces to inhibit bacterial growth.

Shalev, T., Gopin, A., Bauer, M., Stark, R.W., Rahimipour, S.Non-leaching antimicrobial surfaces through polydopamine bio-inspired coating of quaternary ammonium salts or an ultrashort antimicrobial lipopeptide. J. Mater. Chem. 2012, 22, 2026-2032

Yeroslavsky, G., Richman, M., Dawidowicz, L. Rahimipour, S. Sonochemically produced polydopamine nanocapsules with selective antimicrobial activity. Chem. Commun. 2013, 49, 5721-5723 (Cover).

Yeroslavsky G., Girshevitz O., Foster-Frey J., Donovan D.M., Rahimipour S. Antibacterial and antibiofilm surfaces through polydopamine-assisted immobilization of lysostaphin as an antibacterial enzyme. Langmuir 2015, 31, 1064-1073. 

Yeroslavsky G., Lavi R., Alishaev A., Rahimipour S. Sonochemically-produced metal-containing polydopamine nanoparticles and their antibacterial and antibiofilm activity. Langmuir. 2016, 32, 5201-5012.

Yeroslavsky, G. and Rahimipour S. Polydopamine nanocapsules and uses thereof.  Provisional Patent Application 2012

 

Utilizing Multivalency and Supramolecular Chemistry in the Field of Inflammatory Disease Research: Type II Diabetes and Multiple Sclerosis. Various aspects of oxidative cellular stress are associated with the pathogenesis of several devastating human diseases, including diabetes, Alzheimer’s disease, Parkinson’s disease, and multiple sclerosis. It is well known that the generation of reactive oxygen species (ROS) in abnormal amounts or an impairment of the cells’ anti-oxidative protective systems can lead to cellular and tissue damage.

We demonstrated that the multivalent presentation of histidine residues induced by the abiotic self-assembly of cyclic D,L-a-peptides can lead to the generation of multifunctional agents that catalytically decompose intracellular ROS and induce cell protection. In particular, we showed that treatment of muscle cells with such permeable His-rich cyclic peptides protects the cells against the oxidative stress that is induced by hyperglycemic conditions and increases the uptake of glucose from the periphery by increasing the translocation of GLUT1 and GLUT4. In neuronal cells, we were able to show that these peptides exhibit potent anti-inflammatory, anti-oxidant, and anti-excitotoxic activity, and protect the neurons against axonal damage. In a pilot study carried out in collaboration with Teva Pharmaceutical Industries Ltd., we were able to demonstrate that the discovered cyclic peptides exhibit potent neuroprotecting activity in an animal model of multiple sclerosis (experimental autoimmune encephalomyelitis) and significantly ameliorate the related symptoms.

 

Shapira, R., Rudnick, S., Daniel, B., Viskind, O., Aisha, V., Richman, M., Perelman, A., Chill, J. H., Gruzman, A., Rahimipour, S. Multifunctional cyclic D,L-α-peptide architectures stimulate non-insulin dependent glucose uptake in skeletal muscle cells and protect them against oxidative stress, J. Med. Chem. 2013, 56, 6709-6718.

 

Shapiro R. and Rahimipour S. Neuroprotective cyclic peptides, Provisional Patent Application, 2012.

Patents

 

1.   Koch, Y., Fridkin, M., Rahimipour, S. GnRH conjugates comprising a photosensitizer for photodynamic therapy.  PCT Int. Appl. 2004, 59 pp, WO 2004098629, A1 20041118, CAN 141:427990, AN 2004:995998

2.   Koch, Y., Fridkin, M., Rahimipour, S.  Synthesis of long-acting gonadotropin-releasing hormone analogs and therapeutic use thereof.  PCT Int. Appl. 2004, 63 pp, WO 2004030687, A1 20040415, CAN 140:31565, AN 2004:310981

3.    Richman M. and Rahimipour S. Surface modified proteinaceous spherical  particles and  uses thereof, PCT/IB2012/054037


4.    Yeroslavsky, G. and Rahimipour S. Polydopamine nanocapsules and uses thereof.  Provisional Patent Application 2012

Research Group

Current Members:

Dr. Michal Richman, Rresearch Associate

Marina Chemerovsky, Ph.D. Student

Gil Yeroslavsky, Ph.D. Student

Pini Hasin, Ph.D. Student

Elvira Lisniansky, Ph.D. Student

Anna Belostosky, M.Sc. Student

 

Past Members

Sara Wilk

Natalie Skirtenko

Dr. Anna Gopin

Dr. Kamesh Ayasolla

Vered Aisha

Tal Shalev

Guy Leshem

Merav Pasig

Safra Rudnick-Glick

Renana Shapira