Program Faculty Colloquium 2023

8.5.2023, 16:00 / Joseph Loschmidt lecture hall (LH 2) of the Faculty of Chemistry:
Prof. Dr. Peter Burger/ University Hamburg, Germany

http://www.chemie.uni-hamburg.de/ac/burger/index.html

Title: "Activation of H-H, C-H, Si-H and C-C Bonds with Late Transition Metal Pyridine, Diimine Complexes"

Abstract: Non-innocent ligands are a special class of redox-active ligands, which can take up or donate electrons to transition metal centers and can mask their oxidation states. The non-innocent ligands can thus play a cooperative role in the reactivity of the complexes. Our group employs  non-innocent  pyridine,  diimine  ligands  for  late  transition  metal compounds with  multiple bonds to  main-group  elements  M=X  (N,  NR,  S). In the lecture, intra- and  intermolecular C-H, H-H, Si-H and C-C activation processes will be reported, which were analyzed in detail through mechanistic, spectroscopic and theoretical studies.

22.05.2023, 16:00 / Joseph Loschmidt lecture hall (LH 2) of the Faculty of Chemistry:
Assoc.Prof. Dr. Alessio Terenzi/ UNIPA, University of Palermo, Italy

https://pure.unipa.it/en/persons/alessio-terenzi-3

Title: “Multimeric DNA G-quadruplex structures: a promising target for anticancer drugs”

Abstract: G-quadruplexes (G4s) are unique structures in DNA (and RNA) that play a key role inregulating genes and differentiating cells. They are commonly found in cancer-related gene promoters and are considered valuable targets for anticancer drugs. However, most G-rich domains in humans contain multiple adjacent G4 units within long sequences, and current understanding of G4 structures is based on single G4 units derived from short truncated sequences. This could pose a challenge to drug discovery efforts. We (and others) have discovered a clear link between the three G4 units of the KIT promoter, a gene that encodes a tyrosine kinase receptor implicated in multiple malignancies. Our group develops metal complexes to specifically target G4s with a special focus on multimeric quadruplexes.

06.06.2023, 16:00 / Auer von Welsbach lecture hall (LH 1) of the Faculty of Chemistry:
Prof. Dr. Thomas Böttcher/ Faculty of Chemistry, University Vienna

https://boettcher-lab.univie.ac.at/

Title: “Small molecules in a microbial theatre”

Research Areas: The research of Thomas Böttcher focuses on the chemistry of microbial interactions and chemical strategies for modulating microbial growth, virulence, and coordinated behaviours such as swarming motility or biofilm formation. He and his research group are interested in elucidating the chemical structure of metabolites that mediate and control microbe-microbe, microbe-host and microbe-phage interactions and exploit these compounds by synthetic chemistry as species-specific antibiotics and anti-infectives. Furthermore, they develop chemical probes to understand virulence-related functions of human pathogens and develop customized inhibitors of pathogenesis traits. Their goal is to improve the understanding of chemical interactions of microbes and to create chemical tools for precision interventions in complex microbiomes with the ultimate vision of chemical microbiome engineering.

“With our research we will expand the basic understanding of the chemical interactions in the human microbiome and create chemical strategies for the targeted control of microbial pathogens."

12.06.2023, 16:00 / Joseph Loschmidt lecture hall (LH 2) of the Faculty of Chemistry:
Prof. Dr. Donald Hilvert/ ETH Zürich, Switzerland

https://protein.ethz.ch/the-group/group-members/hilvert-donald.html

Title: Evolving virus-like assemblies in the lab

Abstract: Viruses consist of a protective proteinaceous shell that packages an RNA or DNA genome. The emergence of protein cages that could load, protect, and transfer their own genetic information was therefore likely to be a critical step in the evolution of all primitive viruses. Using a combination of design and directed evolution, this process can now be recapitulated in the laboratory.  We have converted a bacterial enzyme called lumazine synthase into an artificial nucleocapsid that efficiently encapsulates its own encoding mRNA and have elucidated the structural changes in cargo and container that made this transformation possible. In addition to providing insight into the origins of natural viruses, such constructs may serve as non-viral carriers for diverse vaccine and delivery applications.