0000000001303980
AUTHOR
W. Bernd Schweizer
showing 5 related works from this author
Fluorine Scan of Inhibitors of the Cysteine Protease Human Cathepsin L: Dipolar and Quadrupolar Effects in the π-Stacking of Fluorinated Phenyl Rings…
2016
The π-stacking of fluorinated benzene rings on protein backbone amide groups was investigated, using a dual approach comprising enzyme-ligand binding studies complemented by high-level quantum chemical calculations. In the experimental study, the phenyl substituent of triazine nitrile inhibitors of human cathepsin L (hCatL), which stacks onto the peptide amide bond Gly67-Gly68 at the entrance of the S3 pocket, was systematically fluorinated, and differences in inhibitory potency were measured in a fluorimetric assay. Binding affinity is influenced by lipophilicity (clog P), the dipole and quadrupole moments of the fluorinated rings, but also by additional interactions of the introduced fluo…
Systematic Investigation of Resorcin[4]arene-Based Cavitands as Affinity Materials on Quartz Crystal Microbalances.
2017
Resorcin[4]arene cavitands are well-known supramolecular hosts, and their outstanding guest-binding abilities in solution have been studied in detail in recent decades. In a systematic approach, different resorcin[4]arene cavitands and container molecules are characterized as affinity materials for gravimetric sensing using high-fundamental-frequency quartz crystal microbalances. Analysis of their affinity toward a series of various analytes reveals a remarkable dependence of both selectivity and sensitivity on the shape, accessibility, and size of the cavity, along with their supramolecular interactions with the host molecules.
Optimization of Triazine Nitriles as Rhodesain Inhibitors: Structure-Activity Relationships, Bioisosteric Imidazopyridine Nitriles, and X-ray Crystal…
2013
The cysteine protease rhodesain of Trypanosoma brucei parasites causing African sleeping sickness has emerged as a target for the development of new drug candidates. Based on a triazine nitrile moiety as electrophilic headgroup, optimization studies on the substituents for the S1, S2, and S3 pockets of the enzyme were performed using structure-based design and resulted in inhibitors with inhibition constants in the single-digit nanomolar range. Comprehensive structure-activity relationships clarified the binding preferences of the individual pockets of the active site. The S1 pocket tolerates various substituents with a preference for flexible and basic side chains. Variation of the S2 subs…
CCDC 916055: Experimental Crystal Structure Determination
2013
Related Article: Veronika Ehmke, Edwin Winkler, David W. Banner, Wolfgang Haap, W. Bernd Schweizer, Matthias Rottmann, Marcel Kaiser, Céline Freymond, Tanja Schirmeister, François Diederich|2013|ChemMedChem|8|967|doi:10.1002/cmdc.201300112
CCDC 916056: Experimental Crystal Structure Determination
2013
Related Article: Veronika Ehmke, Edwin Winkler, David W. Banner, Wolfgang Haap, W. Bernd Schweizer, Matthias Rottmann, Marcel Kaiser, Céline Freymond, Tanja Schirmeister, François Diederich|2013|ChemMedChem|8|967|doi:10.1002/cmdc.201300112