CRC 1093 - Principal Investigator Barbara Saccà

Prof. Barbara Saccà

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Phone: +49 201 183 3097


Centre for Medical Biotechnology
Faculty of Biology
University of Duisburg-Essen

Area A: Chemical Ligands and Methods A6: DNA-based nanocontainers for predesigned spatial confinement of proteins

In A6 prefabricated hexagonal DNA-nanotubes of defined sizes will be equipped with recog-nition labels developed within the CRC and then loaded with selected HtrA proteases, whose biolog-ical role is strictly correlated to their oligomeric state. The altered protein properties will be investi-gated in detail. In the long run, this project will provide a general method which uses supramolecular chemistry for the spatial confinement of minimally modified proteins in engineered DNA-nanochambers, in order to dissect specific biochemical events on a single-molecule scale and gen-erate biomaterials with tailored properties.

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Curriculum Vitae

Professional career

Scientific education and degrees


Selected Publications

A. Sprengel, P. Lill, P. Stegemann, K. Bravo-Rodriguez, E.-C. Schöneweiß, M. Merdanovic, D. Gudnason, M. Aznauryan, L. Gamrad, S. Barcikowski, E. Sanchez-Garcia, V. Birkedal, C. Gatsogiannis, M. Ehrmann  and B. Saccà: Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions. Nat. Commun. 2017, 8, 14472.

E.-C. Schöneweiß and B. Saccà: The collective behavior of spring-like motifs tethered to a DNA origami structure. Nanoscale 2017, 9, 4486-4496.

C. Streich, L. Akkari, C. Decker, J. Bormann, C. Rehbock, A. Müller-Schiffmann, F. C. Niemeyer, L. Nagel-Steger, D. Willbold, B. Saccà, C. Korth, T. Schrader, S. Barcikowski: Characterizing the Effect of Multivalent Conjugates Composed of Aβ-Specific Ligands and Metal Nanoparticles on Neurotoxic Fibrillar Aggregation. ACS Nano 2016, 10, 7582-7597.

W. Pfeifer and B. Saccà: From Nano to Macro through Hierarchical Self-Assembly: the DNA Paradigm. Chembiochem 2016, 17, 1063-1080.

S. Poepsel, A. Sprengel, B. Saccà, F. Kaschani, M. Kaiser, C. Gatsogiannis, S. Raunser, T. Clausen and M. Ehrmann: Determinants of amyloid fibril degradation by the PDZ protease HTRA1. Nat. Chem. Biol. 2015, 1, 862-869.

B. Saccà,* Y. Ishitsuka, R. Meyer, A. Sprengel, E.-C. Schöneweiß, G.U. Nienhaus* and C.M. Niemeyer*: Reversible reconfiguration of DNA origami nanochambers monitored by single-molecule FRET. Angew. Chem. Int. Ed. 2015, 54, 3592-3597. *corresponding authors

B. Saccà, B. Siebers, R. Mayer, M. Bayer and C.M. Niemeyer: Nanolattices of switchable DNA-based motors. Small 2012, 8, 3000-3008.

B. Saccà* and C.M. Niemeyer*: DNA origami: the art of folding DNA. Angew. Chem. Int. Ed. Engl. 2011, 51, 58-66. *corresponding authors

B. Saccà, R. Meyer, M. Erkelenz, K.S. Rabe, K. Kiko, A. Arndt, and C.M. Niemeyer: Orthogonal protein decoration of DNA origami. Angew. Chem. Int. Ed. Engl. 2010, 49, 9378-9383.

Flagged as a “hot” paper.

B. Saccà, R. Meyer and C.M. Niemeyer: Temperature-dependent FRET spectroscopy for the high-throughput analysis of self-assembled DNA nanostructures in real time. Nat. Protoc. 2009, 4, 271-285.