Bioinspired Chemical Engineering Lab



33. Weber, W., Roeder, M., Abujubara, H., Koeppl, H., Tietze, A. A., Stein, V. The functional nanopore (FuN) screen: a versatile genetic assay to study and engineer protein nanopores in Escherichia coli. (2021), DOI: 10.1101/2021.04.20.440580

32. Baumruck, A. C.,  Yang, J.,  Thomas, G.-F.,  Beyer, L. I.,  Tietze, D., Tietze, A. A.*, Native chemical ligation of highly hydrophobic peptides in ionic liquid-containing media. (2021), J. Org. Chem., DOI: 10.1021/acs.joc.0c02498


31. Montoliu Gaya, L., Tietze, D., Kaminski, D., Mirgorodskaya, E., Tietze, A. A., Sterky, F., CA10 regulates neurexin heparan sulfate addition via a direct binding in the secretory pathway (2020), EMBO Reports, DOI: 10.15252/embr.202051349

30. Belyaeva, V.S., Stepenko, Y.V., Lyubimov, I.I., Kulikov, A.L., Tietze, A. A., Kochkarova, I.S., Martynova, O.V., Pokopeyko, O.N., Krupen'kinam l.A., Nagikh, A.S., Pokrovskoy, V.M., Patrakhanov, E.A., Belashova, A.V., Lebedev, P.R., Gureeva, A.V.,* Non-hematopoietic erythropoietin-derived peptides for atheroprotection and treatment of cardiovascular diseases (2020), Research Results in Pharmacology, 6(3), 75-86

29. Müller, L.K.#, Duznovic, I.#, Tietze, D., Weber, W., Ali, M., Stein, V., Ensinger, W., Tietze, A. A.*, Ultrasensitive and selective copper (II) detection: introducing a bioinspired and robust sensor (2020), Chem. Eur. J., 26 (39), 8511-8517, DOI: 10.1002/chem.202001160 

28. Müller, L. K., Baumruck, A. C., Zhdanova, H., Tietze, A. A.*, Challenges and perspectives in chemical synthesis of highly hydrophobic peptides (2020), Front. Bioeng. Biotechnol., 8, 162, DOI: 10.3389/fbioe.2020.00162


27. Korokin, M. V., Soldatov, V. O., Tietze, A. A., Golubev, I. V., Kubekina, M. V., Puchenkova, O. A., Denisyuk, T. A., Gureyev, V. V., Pokrovskaya, T. G., Gudyrev, O. S., Zhuchenko, M. A., Zatolokina, Pokrovskiy, M. V. 11-amino acid peptide imitating the structure of erythropoietin α-helix b improves endothelial function, but stimulates thrombosis in rats (2019), Pharmacy & Pharmacology, 7(6):312-320                                        

26. Tietze, D.*, Batzer-Kaufmann, D., Tietze, A. A., Voll, A., Reher, R., Koenig, G. M., Hausch, F. Structural and dynamical basis of G protein inhibition by YM-254890 and FR900359: an inhibitor in action (2019), J. Chem. Inf. Model., 59 (10), 4361-4373

25. Schöttner, S., Brodrecht, M., Uhlein, E., Dietz, C., Breitzke, H., Tietze, A. A., Buntkowsky, G. and Gallei, M. Amine-containing block copolymers for the bottom-up preparation offunctional porous membranes (2019), Macromolecules, 52, 7, 2631-2641

24. Kaufmann, D. , Tietze, A. A., Tietze, D. In Silico Analysis of the Subtype Selective Blockage of KCNA Ion Channels through the micro-Conotoxins PIIIA, SIIIA, and GIIIA (2019), Marine Drugs, 17 (3), 180

23. Tietze, D.*, Koley Seth, B., Brauser, M., Tietze, A. A., Buntkowsky, G.*, Ni II complex formation and protonation states at the active site of a nickel superoxide dismutase-derived metallopeptide: implications for the mechanism of superoxide degradation (2018), Chemistry,  24, 15879-15888

22. Heimer, P., Baeuml, C.A., Schmitz, T., Resemann, A., Mayer, F.J., Suckau, D., Tietze, A., Ohlenschläger, O., Tietze, D., Imhof, D., Impact of cysteine pairing on disulfide-bond assignment and structure elucidation in different conformational isomers of the µ-conotoxin PIIIA (2018), J. Pept. Sci., 24, S154

21. Steinacker, L., Baumruck, A., Tietze, A.A. Development of a strategic and quantitative route for the chemical synthesis of membrane-associated proteins (2018), J. Pept. Sci., 24, S100

20. Weissheit, S., Kahse, M., Kämpf, K., Tietze, A., Vogel, M., Winter, R., Thiele, C.M., Elastin-like peptide in confinement: FT-IR and NMR T1 relaxation data (2018), Z. Phys. Chem., 232, 7-8, 1239

19. Heimer, P., Tietze, A. A., Bäuml, C. A., Resemann, A., Mayer, F. J., Suckau, D., Ohlenschläger, O., Tietze, D.*, Imhof, D.*, Conformational µ-conotoxin PIIIA isomers revisited: The impact of cysteine pairing on disulfide bond assignment and structure elucidation (2018), Anal. Chem., 90(5), 3321-3327

18. Baumruck, A. C., Tietze, D., Steinacker, L. K., Tietze A. A.*., Chemical synthesis of membrane proteins by native chemical ligation: a model study on the influenza virus B proton channel (2018), Chem. Sci., 9, 2365-2375

17. Leipold, E., Ullrich, F., Thiele, M., Tietze, A. A., Terlau, H., Imhof, D., Heinemann, S. H., Subtype-specific block of voltage-gated K+ channels by μ-conopeptides (2017), Biochem. Biophys. Res. Commun, 482 (4), 1135-1140.

16. Baumruck, A. C., Tietze, D., Stark, A., Tietze, A. A., Reactions of Sulfur-Containing Organic Compounds and Peptides in 1-Ethyl-3-methyl-imidazolium Acetate (2017), J. Org. Chem., 82 (14), 7538–7545 

15. Culbertson, A.T., Tietze, A., Smith, A., Zabotina, O., Three-dimensional structure of Xyloglucan Xylosyltransferase I and proposed methanism of catalysis (2017), FASEB J., 31, 951.4

14. Tietze, D.#, Leipold, E.#, Heimer, P., Böhm, M., Winschel, W., Imhof, D., Heinemann, S.H., and Tietze, A. A.*, Molecular interaction of δ-conopeptide EVIA with voltage-gated Na+ channels, (2016), BBA Gen. Sub., 1860, 2053-2063

13. Culbertson, A.#, Tietze, A. A.#, Tietze, D., Chou, Y.-H., Smith, A. L., Cook, M. D., Young, Z.T., Zabotina, O. A.*, Homology model of a Xyloglucan Xylosyltransferase 2 reveals critical amino acids involved in substrate binding (2016), Glycobiology, 26(9), 961-972

12. Culbertson, A. T., Chou, Y.-H., Smith, A.L., Young, Z.T., Tietze, A. A., Cottaz, S., Faure, R., Zabotina, O.A.*, Enzymatic Activity of Arabidopsis Xyloglucan Xylosyltransferase 5 (2016), Plant Physiol., 171(3), 1893-904

11. Heimer, P.#, Tietze, A. A.#, Böhm, M.#, Giernoth, R., Kuchenbuch, A., Stark, A., Leipold, E., Heinemann, S.H., Kandt, C., Imhof, D.* Application of room temperature aprotic and protic ionic liquids for exidative folding of cysteine-rich peptides (2015), Chem. Biol. Chem. 15, 18, 2754–2765  

10. Böhm, M.#, Tietze, A. A.#, Heimer, P.#, Chen, M., Imhof, D.* Ionic liquids as reaction media for oxidative folding and native chemical ligation of cysteine-containing peptides (2014), J. Mol. Liquids, 192, 67-70  

9. Tietze, A. A.*, Bordusa, F., Giernoth, R., Imhof, D., Lenzer, T., Mrestani-Klaus, C., Neundorf, I., Oum, K., Reith, D., Stark, A., On the nature of interactions between ionic liquids and small amino acid-based biomolecules (2013), Chem. Phys. Chem., 14(18), 4044-64 

8. Tietze, A. A., Tietze, D., Ohlenschläger, O., Ullrich, F., Leipold, E., Heinemann, S.H., Imhof, D., Structurally diverse isomers of a pharmaceurically interesting µ-conotoxin (2013), Biopolymers, 100(3), 260-261

7. Tietze, A. A., Tietze, D., Ohlenschläger, O., Leipold, E., Ullrich, F., Mischo, A., Buntkowsky, G., Görlach, M., Heinemann, S. H., Imhof, D.*, The one and only fold? Structurally diverse µ-conotoxin PIIIA isomers block sodium channel NaV1.4 (2012), Angew. Chem. Int. Ed., 51 (17), 4058-4061

6. Tietze, A. A.*, Heimer, P., Stark, A., Imhof, D., Ionic liquid applications in peptide chemistry: synthesis, purification and analytical characterization processes (2012), Molecules, 17(4), 4158-4185  

5. Miloslavina, A. A., Ebert, C., Tietze, D., Ohlenschläger, O., Englert, C., Görlach, M., Imhof, D.*, An Unusual Peptide from Conus villepinii: Synthesis, Solution Structure, and Cardioactivity (2010), Peptides, 31, 1292-1300

4. Miloslavina, A. A., Stark, A., Imhof, D., Bioactive cysteine-rich peptides are interesting targets for oxidative folding and native chemical ligation in ionic liquids (2010), J. Pept. Sci., 16, 75

3. Leipold, E., Markgraf, R., Miloslavina A. A., Kijas M., Schirmeyer, J., Imhof D., Heinemann S. H.*, Molecular determinant for the subtype specificity of µ-conotoxin SIIIA targeting neuronal voltage-gated sodium channels (2010), Neuropharm., 61 (1-2), 105-111  

2. Miloslavina, A. A., Leipold E., Kijas M., Stark A., Heinemann S.H., Imhof D.* A room temperature ionic liquid as convenient solvent for the oxidative folding of conopeptides (2009), J. Pept. Sci., 15(2), 72-77  

1. Gotfriedsen, J., Miloslavina, A. A., Edelmann, F. T.*, Cyclooctatetraene made easy (2004), Tetrahedr. Lett., 45, 3583-35