Prof. Ehud Gazit

My lab is interested in Molecular Structure and Self-Assembly at the Nano-Scale.

The central dogma in the study of protein folding suggests that the thermodynamically-favorable state of proteins under physiological conditions is their folded one. However, there are number of cases in which the favorable states of proteins are rather unfolded, partially folded (e.g., “molten globular”), or misfolded (e.g., nonspecific aggregates or amyloid fibrils). These observations lead to much interest in the significance and mechanism of formation of such unfolded, misfolded or partially folded structures in physiological as well as pathological conditions.

In our lab we utilize a variety of biochemical, biophysical and molecular biology methodologies to study the mechanism and significance of protein unfolding and misfolding. The experimental systems used are diverse and the partial list includes several bacterial toxin-antidote systems, type II diabetes-related amyloidogenic proteins and peptides, and the VHL tumor suppressor protein. We also study the mechanism of non-specific aggregation of generic unrelated proteins. Another line of research is directed toward the elucidation of the mechanism of action of chemical chaperons and their effect on folding, aggregation and amyloid formation.

For a more details on specific lab activities, please read the full research description.

For the full list

Since 2012

Frydman-Marom A, Convertino M, Pellarin R, Lampel A, Shaltiel-Karyo R, Segal D, Caflisch A, Shalev DE, Gazit E. (2011) Structural basis for inhibiting β-amyloid Oligomerization by a non-coded β-breaker-subtituted endomorphin analogue.ACS Chem Biol. 6, 1265-1276. [Full text in PDF]

Orbach R, Mironi-Harpaz I, Adler-Abramovich L, Mossou E, Mitchell EP, Forsyth VT, Gazit E, Seliktar D. (2012) The rheological and structural properties of Fmoc-peptide-based hydrogels: the effect of aromatic molecular architecture on self-assembly and physical characteristics. Langmuir. 28, 2015-2022 . [Full text in PDF]

Amdursky N, Gazit E, Rosenman G.(2012) Formation of low-dimensional crystalline nucleus region during insulin amyloidogenesis process. Biochem Biophys Res Commun. 419, 232-237. [Full text in PDF]

Amdursky N, Koren I, Gazit E, Rosenman G. (2012) Adjustable photoluminescence of peptide nanotubes coatings. J Nanosci Nanotechnol. 11, 9282-9286.

Scherzer-Attali R, Farfara D, Cooper I, Levin A, Ben-Romano T, Trudler D, Vientrov M, Shaltiel-Karyo R, Shalev DE, Segev-Amzaleg N, Gazit E, Segal D, Frenkel D. (2012) Naphthoquinone-tyrptophan reduces neurotoxic Aβ*56 levels and improves cognition in Alzheimer's disease animal model. Neurobiol Dis. 46, 663-72. [Full text in PDF]

Scherzer-Attali, R., Shaltiel-Karyo, R., Adalist, Y. H., Segal, D., and Gazit E. (2012) Generic inhibition of amyloidogenic proteins by two naphthoquinone-tryptophan hybrid molecules.   Proteins 80 , 1962-1973.

Shaltiel-Karyo, R., Davidi, D., Frenkel-Pinter, M., Ovadia, M., Segal, D., and Gazit E. (2012) Differential inhibition of α-synuclein oligomeric and fibrillar assembly in parkinson's disease model by cinnamon extract.   Biochim. Biophys. Acta.  1820 , 1628-1635.

Adler-Abramovich L, Vaks L, Carny O, Trudler D, Magno A, Caflisch A, Frenkel D, Gazit E. (2012) Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.   Nature Chem. Biol.   8, 701-706.

Goldshtein, K., Golodnitsky, D., Peled, E. Adler-Abramovich, L., Gazit, E., Khatun, S., Stallworth, P. and Greenbaum, S. (2012) Effect of peptide nanotube filler on structural and ion-transport properties of solid Polymerelectrolytes.   Solid State Ionics.   220 , 39–46.

Shaltiel-Karyo, R., Davidi, D., Menuchin, Y., Frenkel-Pinter, M., Marcus-Kalish, M., Ringo, J., Gazit, E., and Segal, D. (2012) A novel, sensitive assay for behavioral defects in Parkinson's disease model Drosophila. Parkinsons Dis. 2012 : 697564.

Herzog, G., Joerger, A.C., Shmueli, M.D., Fersht, A.R., Gazit, E., and Segal, D. (2013) Evaluating Drosophila p53 as a model system for studying cancer mutations. J. Biol. Chem. 287 , 44330-44337.

Scherzer-Attali, R., Convertino, M., Pellarin, R., Gazit, E., Segal, D., and Caflisch, A. (2013) Methylations of tryptophan-modified naphthoquinone affect its inhibitory potential toward Aβ aggregation. J. Phys. Chem. B. 117 , 1780-1789.

Ischakov, R., Buzhansky, L., Adler-Abramovich, L., & Gazit, E. (2013) Peptide-Based Hydrogel Nanoparticles as Effective Drug Delivery Agents. Bioorg. Med. Chem. 21 , 3517-3522

Lampel, A., Bram, Y., Levy-Sakin, M., Bacharach, E., & Gazit, E. (2013) The Effect of Chemical Chaperones on the Assembly and Stability of HIV-1 Capsid Protein. PLoS One 8, e60867.

Ghosha, S., Adler-Abramovich, L., Gazit, E.* , & Verma, S*. (2013) Spacer Driven Morphological Twist in Phe-Phe Dipeptide Conjugates. Tetrahedron 69 , 2004-2009. *Both Corresponding authors.

Shaltiel-Karyo, R., Frenkel-Pinter, M., Rockenstein, E., Patrick, C., Levy-Sakin, M., Schiller, A., Egoz-Matia, N., Masliah, E., Segal, D., & Gazit, E. (2013) A Blood-Brain Barrier (BBB) Disrupter is also a Potent α-Synuclein (α-syn) Aggregation Inhibitor: A Novel Dual Mechanism of Mannitol for the Treatment of Parkinson Disease (PD). J. Biol. Chem. 288 , 17579-17588.

Lampel, A., Yaniv, O., Berger, O., Bacharach, E., Gazit, E. , & Frolow, F. (2013) A Triclinic Crystal Structure of the Carboxy-Terminal Domain of HIV-1 Capsid Protein with Four Molecules in the Asymmetric Unit Reveals a Novel Packing Interface. Acta Crystallogr. Sect. F. 69 , 602-606.

Shmueli, M.D., Schnaider, L., Rosenblum, D., Herzog, G., Gazit, E. , & Segal D. (2013)  Structural Insights into the Folding Defects of Oncogenic pVHL Lead to Correction of its Function In Vitro. PLoS One 8 , e66333 7 .

Davidi, D., Sade, D., Schuchalter, S., & Gazit, E. (2014) High Throughput Assay for Temporal Kinetic Analysis of Lytic Coliphages Activity. Anal. Biochem. 444 , 22-24.

Fichman, G., & Gazit, E. (2014) Self-Assembly of Short Peptides to Form Hydrogels: Design of Building Blocks, Physical Properties and Technological Applications. Acta Biomater. 10 , 1671-1682.

Azuri, I., Adler-Abramovich, L., Gazit, E. , Hod, O., & Kronik, L. (2014) Why are Diphenylalanine-Based Peptide Nanostructures so Rigid? Insights from First Principles Calculations. J. Am. Chem. Soc. 136 , 963-969.

Vasudev, M. C., Koerner, H., Singh, K. M., Partlow, B. P., Kaplan, D. L., Gazit, E. , Bunning, T. J., & Naik, R. R. (2014). Vertically Aligned Peptide Nanostructures Using Plasma-Enhanced Chemical Vapor Deposition. Biomacromolecules 15 , 533-540.

Mason, T. O., Chirgadze, D. Y., Levin, A., Adler-Abramovich, L., Gazit, E. , Knowles, T. P., & Büll, A. K. (2014) Expanding the Solvent Chemical Space for Self-Assembly of Dipeptide Nanostructures. ACS Nano 8 , 1243-1253.

Levy-Sakin, M., Berger, O., Feibish, N., Sharon, N., Schnaider, L., Shmul, G., Amir, Y., Buzhansky, L., & Gazit, E. (2014) The Influence of Chemical Chaperones on Enzymatic Activity under Thermal and Chemical Stresses: Common Features and Variation among Diverse Chemical Families. PLoS One 9 , e88541.

Mossou, E., Teixeira, S. C. M., Mitchell, E.P., Mason, S.A., Adler-Abramovich, L., Gazit, E. , & Forsyth, V. T. (2014) Crystal Structure of the Self-Assembling Zwitterionic Form of Phenylalanine at Neutral pH. Acta Crystallogr. Sect. C. 70 , 326-331.

Bram, Y., Frydman-Marom, A., Yanai, I., Gilead, S., Shaltiel-Karyo, R., Amdursky, A., & Gazit, E. (2014) Apoptosis Induced by Islet Amyloid Polypeptide Soluble Oligomers is Neutralized by Diabetes-Associated Specific Antibodies. Sci. Rep.4 , 4267.

Fichman, G., Adler-Abramovich, L., Manohar, S., Mironi-Harpaz, I., Guterman, T., Seliktar, T., Messersmith, P., & Gazit, E. (2014) Seamless Metallic Coating and Surface Adhesion of Self-Assembled Bioinspired Nanostructures Based on Di-(3,4-dihydroxy-l-phenylalanine) Peptide Motif. ACS Nano 8 , 7220-7228 (Featured in the cover of the issue).

Fichman, G., Guterman, T., Adler-Abramovich, L., & Gazit, E. (2014) The Use of the Calcitonin Minimal Recognition Module for the Design of DOPA-Containing Fibrillar Assemblies. Nanomaterials 4 , 726-740.

Gazit, E. (2014) Controlling Molecular Self-assembly: From Amyloid Oligomerization and Therapy to Novel Biomaterials and Technological Applications. Nanomedicine (in press).

Adler-Abramovich, L., & Gazit, E. (2014) The Physical Properties of Supramolecular Peptide Assemblies: From Building Block Association to Technological Applications. Chem. Soc. Rev. 43 , 6881-6893 (Featured in the cover of the issue).

Shmueli, M. D., Schnaider, L., Herzog, G., Gazit, E. , and Segal, D. (2014) Computational and experimental characterization of dVHL establish a Drosophila model of VHL syndrome. PLoS One 9 , e109864.

Levin, A. Mason, T. O., Adler-Abramovich, L., Buell, A. K., Meisl, G., Galvagnion, C., Bram, Y., Dobson, C. M., Knowles, T. P. J., & Gazit, E. (2014) Ostwald’s Rule of Stages Governs Structural Transitions and Morphological Control of a Dipeptide Supramolecular Polymer. Nature Commun. (in press).