פרופ' אילה למפל

Prof. Ayala Lampel is an Associate Professor in the Shmunis School of Biomedicine and Cancer Research at Tel Aviv University. She started her academic appointment as an Assistant Professor at Tel Aviv University in 2019. She obtained a PhD in Biotechnology and a BSc in Neuroscience from Tel Aviv University.

Education:

2015-2019       Postdoctoral fellow, Nanoscience Initiative, Advanced Science Research Center, City University of New York

2009-2014       Ph.D., Direct track in Biotechnology, Department of Molecular Microbiology and Biotechnology, Tel Aviv University

2005-2008       B.Sc., Neuroscience, Tel Aviv University

Academic appointments:

2024       Associate Professor, Tel Aviv University

2019       Assistant Professor, Tel Aviv University

Designing synthetic organelles formed through liquid-liquid phase separation (LLPS), capable of encapsulating various payloads for applications in drug delivery, sensing, and catalysis

Specific interests:

- Design of synthetic organelles and biomolecular condensates with tunable properties

- Phase-separated materials for biocatalysis and green chemistry

- Synthetic organelles as enzymatic microreactors

- Designed condensates as delivery platforms

- Peptide materials for biosensing applications

Lampel, A., Tuttle, T., Ulijn, R.V. Guiding principles for peptide nanotechnology through directed discovery. Chemical Society Reviews. 2018, 47, 3737-3758.

Zhang, C., Shafi, R., Lampel, A., MacPherson, D., Pappas, C. G., Wang, T.,  Maldarelli C., Ulijn, R. V. Switchable Hydrolase Based on Reversible Formation of Supramolecular Catalytic Site Using a Self‐Assembling Peptide. Angewandte Chemie International Edition. 2017, 129, 14703-14707.

Lampel, A., McPhee S. A., Park, H.-A. Scott, G. G., Humagain, S., Hekstra, D. R., Yoo, B., Frederix P. W. J. M., Li, T.-D., Abzalimov R. R., Greenbaum S. G., Tuttle, T., Chunhua H., Bettinger, C. J., Ulijn, R. V. Polymeric peptide pigments with sequence-encoded properties. Science 2017, 356, 1064-1068.

Alakpa, E. V., Jayawarna, V., Lampel, A., Burgess, K. V., West, C. C., Bakker, S. C.J, Roy, S., Javid, N., Fleming, S., Lamprou, D. A., Yang, J., Miller, A., Urquhart, A. J, Frederix, P. W.J.M., Hunt, N. T, Péault, B., Ulijn, R. V., Dalby, M. J. Tunable supramolecular hydrogels for selection of lineage guiding metabolites in stem cell cultures. Chem 2016, 1, 298-319.

Lampel, A., Varenik M., Regev O., Gazit, E. Hierarchical multi-step organization during viral capsid assembly. Colloids and Surfaces B: Biointerfaces 2015, 136, 674-677.

Mondal, S*., Adler-Abramovich, L*., Lampel, A., Bram, Y., Lipstman, S., Gazit, E. Formation of functional super-helical assemblies by constrained single heptad repeat. Nature Communications 2015, 6.

Lampel, A., Bram, Y., Ezer A., Shaltiel-Kario R., Saad, J. S., Bacharach, E., Gazit, E. Targeting the early step of building block organization in viral capsid assembly. ACS Chemical Biology 2015, 10, 1785-1790.

Lampel, A., Elis E., Guterman, T., Shapira S., Marco, P., Bacharach, E., Gazit, E. α-Aminoisobutyric acid incorporation induces cell permeability and antiviral activity of HIV-1 major homology region fragments. Chemical Communications 2015, 51, 12349-12352.

Bram, Y., Lampel, A., Shaltiel-Karyo, R., Ezer, A., Scherzer-Attali, R., Segal, D., Gazit, E. Monitoring and targeting the initial dimerization stage of amyloid self-assembly. Angewandte Chemie International Edition 2014, 54, 2062-2067.

Lampel, A., Yaniv, O., Berger, O., Bacharach, E., Gazit, E., Frolow, F. 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 Crystallographica Section F 2013, F69, 602-606.

Lampel, A., Bram, Y., Levy-Sakin, M., Bacharach, E., Gazit, E. The effect of chemical chaperones on the assembly and stability of HIV-1 capsid protein. PLOS ONE 2013, 8(4): e60867.

Frydman-Marom, A., Convertino, M., Pellarin, R., Lampel, A., Shaltiel-Kario, R., Caflisch, C., Shalev, E. D., Gazit, E. Structural basis for inhibiting β-amyloid oligomerization by a non-coded β-breaker-substituted endomorphin analogue. ACS Chemical Biology 2011, 6, 1265-1276.