Dr. Ayala Lampel is an assistant professor (senior lecturer) in the School of Molecular Cell Biology and Biotechnology since 2019. She obtained a B.Sc. in Neuroscience and a PhD in Biotechnology from Tel Aviv University.
Dr. Ayala Lampel
Faculty of Life Sciences
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
2019 Assistant Professor, Tel Aviv University
Biological systems use a precise control in space and time to form functional materials, however, their dynamic properties are not yet accessible in man-made biomaterials. Our vision is to fill this gap by studying the manufacturing process of biological materials used in nature and applying these insights into design tools for biomaterials.
- Compartmentalization of enzymatic reactions in synthetic organelles;
- Molecular self-assembly of ordered/disordered peptide and protein structures and their biophysical characterization;
- Design rules of peptide assemblies as models for membraneless organelles;
- Design of dynamic bioreactors formed by multicomponent peptide-based building blocks;
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.