Roman Jerala

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National Institute of Chemistry
Jerala, Roman

Roman Jerala  Department of Biotechnology @National institute of Chemistry in Ljubljana, Slovenia    

BSc and PhD in chemistry (1993), University of Ljubljana, Slovenia  postdoc U.Virginia 1994-1995  since 2002 head of Department of biotechnology, NIC  since 2009 director of synthetic biology area at Centre of excellence EN-FIST    

Research interests:  – synthetic biology (iGEM team leader since 2006): mammalian cell engineering, information processing in cells, medical applications, bionanomaterials  – molecular mechanisms of innate immunity

Wed July 10 | 2:00 - 4:00 | Parallel Session
ABSTRACT: Protein origami based on modular coiled-coil interactions

Proteins  are able to perform versatile functions due to the variability of aminoacid side chains and their tertiary structures that  evolved through complex cooperative interactions.  De novo protein fold design  is still very challenging. We devised a strategy to design self-assembling polypeptide nanostructured polyhedra, based on orthogonal coiled-coil dimerizing mudular segments. We designed end experimentally demonstrated formation of the tetrahedron that self-assembles from a single polypeptide chain comprising 12 concatenated coiled-coil-forming segments connected by flexible peptide hinges. Path of the polypeptide chain is guided by the defined order of segments that traverse each of the 6 edges of the tetrahedron exactly twice, forming coiled-coil dimers with their corresponding partner segments. WE demonstrated formation of discrete particles in agreement with designed shape using CD, DLS, imaing by electron microscopy and AFM. Coincidence of the polypeptide termini in the same vertex was demonstrated by reconstitution of the split fluorescent protein by the polypeptide with the correct tetrahedral topology, while polypeptides with a deleted or scrambled segment order fail to self-assemble correctly. This design platform provides the basis for construction of new topological polypeptide folds based on the set of orthogonal interacting polypeptide segments.