Liberty Blue Customer Highlight: Dr. Monika Szefczyk
Dr. Monika Szefczyk,is a researcher in the lab of Professor Berlicki in the Department of Bioorganic Chemistry at Wrocław University of Science and Technology. She met with CEM to discuss their research into peptide foldamers, most recently applying them to SARS-Cov-2 inhibition. Dr. Berlicki’s laboratory owns a CEM Liberty Blue microwave peptide synthesizer
Q: Could you provide some background on the Berlicki research group?A: Berlicki Lab is one of the 5 research groups of the Department of Bioorganic Chemistry, Wrocław University of Science and Technology. It is headed by Professor Łukasz Berlicki and consists of 7 researchers and 3 PhD students. Our research is focused on three main topics: 1) structure, biological and catalytic activity of peptide foldamers, 2) synthesis and activity of inhibitors of chosen enzymes and 3) peptide-based nanostructures. We are leading 5 ongoing research projects financed by the National Science Center and the Polish National Agency for Academic Exchange for a total amount of more than PLN 5 million.
Q: What are your key research goals?A: We mainly work on peptide foldamers - oligomers that exhibit a high tendency to fold into stable three-dimensional structures in solution. The possibility of rational construction of structurally extended molecules gives chance to create materials with numerous functionalities. The development of rational strategy for the obtaining of extended protein-like foldameric structures (so-called foldameric mini-proteins) is one of our primary goals. Subsequently, we apply the obtained structures for construction of molecules exhibiting catalytic or biological activities. Building enzyme mimetics provide catalysts for various reactions as well as allows better understanding of the action of native enzymes. Moreover, we are synthesizing protein-protein interaction inhibitors that are potentially useful in cancer immunotherapy. Recently, we focused on the group of peptide foldamers that would be able to inhibit the interaction of human ACE2 and SARS-Cov-2 virus S protein. Such compounds could stop virus entry to human cells and may be candidates for drugs against Covid-19.
We also focus on another interesting aspect of peptide foldamers, namely their ability to form nanostructures as a result of controlled self-aggregation. We designed, synthesized and characterized various peptides containing beta-amino acids and used them to obtain nanofibrils in the process of self-association. Now we endeavor to develop different microscopic techniques dedicated to characterization of obtained nanostructures and bionanomaterials in general. Sequence Engineering to Control the Helix Handedness of Peptide Foldamers
Q: How has the Liberty Blue improved your research?A: Most importantly, the Liberty Blue has allowed us to significantly reduce synthesis time and diminish the cost of solvent and the waste production in comparison to other automated synthesizers. In our case the difference is significant taking into account a large number of peptides with long sequences that we synthesize in our lab. Moreover, we were able to easily optimize the synthesis of peptides with so-called “difficult sequences”.
Q: Do you think the Liberty Blue could be useful to other scientists?A: We would recommend the Liberty Blue as an easy to use, time and cost saving synthesizer, enabling us to obtain peptides with good yield and purity. The availability of professional support from the CEM technical specialist is also worth mentioning.
Q: Where should chemists look for further reading on your research?A: We are on Facebook and Twitter @berlickilab. For more information, please see also the webpage of our Department: http://bioorganic.ch.pwr.wroc.pl/ or the selected publications below.
- Fortuna, P.; Linhares, B. M.; Purohit, T.; Pollock, J.; Cierpicki, T.; Grembecka, J.; Berlicki, Ł., Covalent and noncovalent constraints yield a figure eight-like conformation of a peptide inhibiting the menin-MLL interaction Eur. J. Med. Chem. 2020, 207, 112748. View at Publisher
- Drewniak, M.*; Węglarz-Tomczak, E*; Ożga, K.; Rudzińska-Szostak, E.; Macegoniuk, K.; Tomczak, J. M.; Bejger, M.; Rypniewski, W.; Berlicki, Ł. *contributed equally., Helix-loop-helix peptide foldamers and their use in the construction of hydrolase mimetics. Bioorg. Chem. 2018, 81, 356. View at Publisher
- Szefczyk, M.; Węglarz-Tomczak, E.; Fortuna, P.; Krzysztoń, A.; Rudzińska-Szostak, E.; Berlicki, Ł., Controlling the Helix Handedness of ααβ-Peptide Foldamers through Sequence Shifting Angew. Chem. Int. Ed. 2017, 56, 2087. View at Publisher
- Rudzińska-Szostak, E.; Berlicki, Ł., Sequence engineering to control the helix handedness of peptide foldamers Chem. Eur. J. 2017, 23, 14980. View at Publisher
- Magiera-Mularz, K.; Skalniak, L.; Zak, K. M.; Musielak, B.; Rudzinska-Szostak, E.; Berlicki, Ł.; Kocik, J.; Grudnik, P.; Sala, D. Zarganes-Tzitzikas, T.; Shaabani, S.; Dömling, A.; Dubin, G.; Holak, T. A., Bioactive Macrocyclic Inhibitors of the PD-1/PD-L1 Immune Checkpoint Angew. Chem. Int. Ed. 2017, 56, 13732. View at Publisher
photo top credit: materials from Wroclaw Technical University