Miriam Böhm
University of Bonn
6 Papers
91 Citations
Miriam Böhm is an academic researcher from University of Bonn. The author has contributed to research in topics: Ionic liquid & Peptide. The author has an hindex of 5, co-authored 6 publications.
Chat about Author
Papers
Synthesis and Functional Characterization of Tridegin and Its Analogues: Inhibitors and Substrates of Factor XIIIa
Miriam Böhm,Toni Kühl,Toni Kühl,Kornelia Hardes,Richard Coch,Christoph Arkona,Bernhard Schlott,Torsten Steinmetzer,Diana Imhof +8 more
TL;DR: The chemical synthesis of tridegin is described by two different strategies—solid‐phase assembly and native chemical ligation—both followed by oxidation in solution phase, which revealed that the glutamine residue at position 52 (Q52) oftridegin most likely binds to the active site of factor XIIIa and was therefore suggested to react with the enzyme.
28
Application of Room‐Temperature Aprotic and Protic Ionic Liquids for Oxidative Folding of Cysteine‐Rich Peptides
Pascal Heimer,Alesia A. Tietze,Miriam Böhm,Ralf Giernoth,Andrea Kuchenbuch,Annegret Stark,Enrico Leipold,Stefan H. Heinemann,Christian Kandt,Diana Imhof +9 more
TL;DR: The oxidation of the conotoxin μ‐SIIIA in different ionic liquids was investigated, and the results were compared with those obtained in [C2mim][OAc], where a significant loss of the effect on ion channel NaV1.4 relative to the buffer‐oxidized peptide was revealed.
23
Ionic liquids as reaction media for oxidative folding and native chemical ligation of cysteine-containing peptides
TL;DR: It is found that imidazolium-based ionic liquids, and more precisely [C2mim][OAc], were most suitable for both reactions being superior to conventional aqueous buffer systems in several aspects, including reaction yield and time, concentration of starting material and product as well as selectivity.
19
Novel insights into structure and function of factor XIIIa-inhibitor tridegin.
Miriam Böhm,Charlotte A. Bäuml,Kornelia Hardes,Torsten Steinmetzer,Dirk Roeser,Yvonne Schaub,Manuel E. Than,Arijit Biswas,Diana Imhof +8 more
TL;DR: Molecular modeling and docking studies confirm disulfide bond isomer preference with respect to binding to FXIIIa, and knowledge of the enzyme-inhibitor interactions might bring about comprehensive ideas for the design of a suitable lead structure for addressingFXIIIa.
19
Molecular interaction of δ-conopeptide EVIA with voltage-gated Na(+) channels.
Daniel Tietze,Enrico Leipold,Pascal Heimer,Miriam Böhm,Wadim Winschel,Diana Imhof,Stefan H. Heinemann,Alesia A. Tietze +7 more
TL;DR: The prototypical voltage-sensor toxin δ-EVIA is suited for the elucidation of its binding epitope and in-depth analysis of its interaction with the channel target yields information on the mode of action and might also help to unravel the mechanism of voltage-dependent channel gating and coupling of activation and inactivation.
12