Sandro Tonazzi


PhD Student


HCI G-306


+41-44-633 4168


Sandro Tonazzi



Apprenticeship for Laboratory Assistant (NOVARTIS) and professional maturity.


Job in Industry as Laboratory Assistant (Syngenta).


Diploma Studies in Chemistry at FHNW (Muttenz).


Diploma Thesis with Prof. E. Hungerbühler (FHNW) and Prof. H. Wennemers (University of Basel, awarded with the Diplompreis of NOVARTIS).


MSc Studies of Chemistry, ETH Zürich.


Master Thesis with Prof. F. Diederich (ETH Zürich).

since 2009:

PhD with Prof. F. Diederich (ETH Zürich).

Structure-Based Design and Synthesis of Inhibitors for Arylsulfate Sulfotransferase (ASST); on a quest for new antibiotics in case of urinary tract infections

The crystal structure of the PAPS-independent arylsulfate sulfotransferase (ASST) could be solved only recently in the year 2008 after isolation from uropathogenic Escherichia coli (G. Malojcic, Proc. Nat. Acad. Sci. U. S. A. 105, 19217-19222). ASSTs catalyse the transfer of a sulfuryl group from an activated donor to an acceptor. In doing so, many physiological processes can be initiated and carried out, e.g. the detoxification of medically active compounds such as antibiotics. Since uropathogenic Escherichia coli (UPEC) can cause urinary tract infections (UTI), ASST represents an attractive target for the treatment of UTI. We are thus trying to inhibit this highly polar binding site of ASST in order to develop new antibiotics and to gain insight into the binding mode, by investigating the various interactions of the synthesized inhibitors with the active site of ASST.

Figure 1: Dimer of ASST which catalyses the PAPS-independent transfer of sulfurylgroups within uropathogenic Escherichia coli.


M. Wiesner, J. D. Revell, S. Tonazzi, H. Wennemers, J. Am. Chem. Soc. 2008, 130, 5610-5611. Peptide catalyzed asymmetric conjugate addition reactions of aldehydes to nitroethylene - A convenient entry into gamma(2)-amino acids.

Last update: Dec. 2009.