Adrian Glas
Max Planck Society
14 Papers
51 Citations
Adrian Glas is an academic researcher from Max Planck Society. The author has contributed to research in topics: Peptidomimetic & Peptide binding. The author has an hindex of 9, co-authored 14 publications. Previous affiliations of Adrian Glas include Technical University of Dortmund.
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Papers
Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes
TL;DR: A new classification of peptidomimetics (classes A–D) is introduced that enables a clear assignment of available approaches for the structure-based design of PPI inhibitors through stabilizing or mimicking turns, β-sheets, and helices.
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Constrained Peptides with Target‐Adapted Cross‐Links as Inhibitors of a Pathogenic Protein–Protein Interaction
TL;DR: This work presents a rational approach towards stabilization of an irregular peptide structure, using hydrophobic cross-links that replace residues crucially involved in target binding in peptide-derived PPI inhibitors.
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Targeting β-catenin dependent Wnt signaling via peptidomimetic inhibitors in murine chondrocytes and OA cartilage.
A. Held,Adrian Glas,Laura Dietrich,M. Bollmann,K. Brandstädter,Tom N. Grossmann,Christoph H. Lohmann,Thomas Pap,Jessica Bertrand +8 more
TL;DR: Data indicate that blockade of canonical Wnt signaling might be a therapeutic strategy to treat early OA cases and protect further cartilage degradation by preventing chondrocyte hypertrophic differentiation.
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Increased Conformational Flexibility of a Macrocycle-Receptor Complex Contributes to Reduced Dissociation Rates.
Adrian Glas,Eike-Christian Wamhoff,Eike-Christian Wamhoff,Dennis M. Krüger,Dennis M. Krüger,Christoph Rademacher,Christoph Rademacher,Tom N. Grossmann,Tom N. Grossmann +8 more
TL;DR: Report of unexpected trends in the binding kinetics of two closely related macrocyclic peptides that bind their receptor protein with high affinity reveals that increased conformational flexibility of the macrocycle–receptor complex reduces dissociation rates and contributes to complex stability.
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Structure‐Based Design of Inhibitors of Protein—Protein Interactions: Mimicking Peptide Binding Epitopes
TL;DR: In this paper, a classification of peptidomimetics (classes A-D) is introduced to enable a clear assignment of available approaches for the structure-based design of PPI inhibitors.
21