Raz Jelinek, Ph.D
Ben-Gurion University, Beer Sheva, Israel

Raz Jelinek got his B.Sc. degree in chemistry (S.c.L.) from the Hebrew University in Jerusalem.  He then obtained his Ph.D.  in chemistry at the University of California, Berkeley, working under the guidance of Professor Alex Pines to develop and apply advanced methods of solid-state NMR spectroscopy.  Dr. Jelinek then moved to the University of Pennsylvania where he was a Cancer Research Institute post-doctoral fellow, working on applications of NMR spectroscopy to studying epitope/antibody interactions.  Since 1996, Dr. Jelinek has been a faculty member at the Department of Chemistry, Ben-Gurion University, Beer Sheva, Israel, where he is currently a Full Professor.  Research in his laboratory is broad-based and spans nanotechnology, surfaces and thin films, sensors, and biological membranes.  The research activity in the laboratory has a certain applied-science emphasis, which several patents awarded/pending.  Current projects involve self-assembled functional Au coatings in 2D and 3D through the use of a novel Au nanoparticle precursor; construction of organized structures at the air/water interface; chromatic sensors for biological and chemical molecules based upon polydiacetylene – a unique conjugated polymer; membrane interactions of amyloidoenic peptides; and amphiphilic carbon quantum dots.

The Jelinek group is aiming to decipher the molecular mechanisms for the inhibition action of the molecular tweezers, particularly in the context of membrane interactions of the amyloid β-protein (Aβ). This information could be crucial, since many studies have linked the pathological/toxic effects of Aβ to the cellular membrane. A recent study (1) in the Jelinek laboratory has analyzed the impact of the molecular tweezer, CLR01, on membrane interactions of Aβ42, the longer form of Aβ. Interestingly, CLR01 was found to have significant interaction with membranes itself. However, the membrane bilayer disruption by Aβ42 was reduced when the harmful peptide was incubated with the molecular tweezer (Figure 1), suggesting that binding of CLR01 to Aβ42 attenuated its membrane interactions.
Figure 1. CLR01 protects artificial lipid vesicles from disruption by Aβ42. The figure shows lipid vesicles labeled by novel fluorescent “carbon dots” developed in the Jelinek laboratory. In a undisrupted vesicle, the carbon dots are dispersed evenly, whereas Aβ42 causes clustering of the dots in one main spot. CLR01 partially reverses this effect of Aβ42.

Reference:

  1. R Malishev, S Nandi, S Kolusheva, Y Levi-Kalisman, F-G Klärner, T Schrader, G Bitan, and R Jelinek (2015) Toxicity inhibitors protect lipid membranes from disruption by Aβ42, ACS Chem. Neurosci. 6: 1860-1869.