Leon Wehrhan
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View article: Fluorinated Protein–Ligand Complexes: A Computational Perspective
Fluorinated Protein–Ligand Complexes: A Computational Perspective Open
Fluorine is an element renowned for its unique properties. Its powerful capability to modulate molecular properties makes it an attractive substituent for protein binding ligands; however, the rational design of fluorination can be challen…
View article: Prebound State Discovered in the Unbinding Pathway of Fluorinated Variants of the Trypsin–BPTI Complex Using Random Acceleration Molecular Dynamics Simulations
Prebound State Discovered in the Unbinding Pathway of Fluorinated Variants of the Trypsin–BPTI Complex Using Random Acceleration Molecular Dynamics Simulations Open
The serine protease trypsin forms a tightly bound inhibitor complex with the bovine pancreatic trypsin inhibitor (BPTI). The complex is stabilized by the P1 residue Lys15, which interacts with negatively charged amino acids at the bottom o…
View article: Pre-bound State Discovered in the Unbinding Pathway of Fluorinated Variants of the Trypsin-BPTI Complex Using Random Acceleration Molecular Dynamics Simulations
Pre-bound State Discovered in the Unbinding Pathway of Fluorinated Variants of the Trypsin-BPTI Complex Using Random Acceleration Molecular Dynamics Simulations Open
The serine protease trypsin forms a tightly bound inhibitor complex with Bovine Pancreatic Trypsin Inhibitor (BPTI). The complex is stabilized by the P1 residue Lys15, which interacts with the negatively charged amino acids at the bottom o…
View article: Biosynthetic incorporation of fluorinated amino acids into the nonribosomal peptide gramicidin S
Biosynthetic incorporation of fluorinated amino acids into the nonribosomal peptide gramicidin S Open
Since fluorinated compounds are vital in medicinal chemistry, incorporating fluorine into natural products is attracting interest. We enable incorporation of 4-fluoro-Phe into the nonribosomal peptide gramicidin S with a surgical mutation.
View article: A Formylglycine‐Peptide for the Site‐Directed Identification of Phosphotyrosine‐Mimetic Fragments**
A Formylglycine‐Peptide for the Site‐Directed Identification of Phosphotyrosine‐Mimetic Fragments** Open
Discovery of protein‐binding fragments for precisely defined binding sites is an unmet challenge to date. Herein, formylglycine is investigated as a molecular probe for the sensitive detection of fragments binding to a spatially defined pr…
View article: Water Network in the Binding Pocket of Fluorinated BPTI-Trypsin Complexes - Insights from Simulation and Experiment
Water Network in the Binding Pocket of Fluorinated BPTI-Trypsin Complexes - Insights from Simulation and Experiment Open
Structural waters in the S1 binding pocket of β -trypsin are critical for the stabilization of the complex of β -trypsin with its inhibitor bovine pancreatic trypsin inhibitor (BPTI). The inhibitor strength of BPTI can be modulated by repl…
View article: CCDC 2157920: Experimental Crystal Structure Determination
CCDC 2157920: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: A Formylglycine-Peptide for the Site-Directed Identification of Phosphotyrosine-Mimetic Fragments
A Formylglycine-Peptide for the Site-Directed Identification of Phosphotyrosine-Mimetic Fragments Open
Discovery of protein-binding fragments for precisely defined binding sites is an unmet challenge so far. Here, we investigate formylglycine as a molecular probe for the sensitive detection of fragments binding to a spatially defined protei…
View article: Pentafluorophosphato‐Phenylalanines: Amphiphilic Phosphotyrosine Mimetics Displaying Fluorine‐Specific Protein Interactions
Pentafluorophosphato‐Phenylalanines: Amphiphilic Phosphotyrosine Mimetics Displaying Fluorine‐Specific Protein Interactions Open
Phosphotyrosine residues are essential functional switches in health and disease. Thus, phosphotyrosine biomimetics are crucial for the development of chemical tools and drug molecules. We report here the discovery and investigation of pen…
View article: Front Cover: Druggability Assessment for Selected Serine Proteases in a Pharmaceutical Industry Setting (ChemMedChem 21/2020)
Front Cover: Druggability Assessment for Selected Serine Proteases in a Pharmaceutical Industry Setting (ChemMedChem 21/2020) Open
The Front Cover shows the backbone representation of a protein structural ensemble for the serine protease FXa with a reticle pointing at it. The potential of targeting a protein with a drug-like molecule plays an important role in early d…