Thinking Outside the Binding Site: A Self‐Encapsulating Kinase Inhibitor Remodels Its Pocket to Achieve Selectivity

ABSTRACT Rendering kinase inhibitors selective is a strict requirement in drug development and remains a persistent challenge. To identify new routes to engineer selectivity, we have discovered a first‐in‐class p38δ‐isoform selective inhibitor reflecting 12 000‐fold selectivity improvement over currently available compounds and superior kinome targeting. X‐ray crystallographic characterization indicates that these molecules bind through noncanonical n–π–π stacking sandwich interactions enabled by structural remodeling of the P‐loop. Structural and functional analysis indicates that these selective inhibitors are self‐encapsulating agents due to direct steric clashing that occludes the binding site in a conformation reinforced by a hydrogen‐bonding network involving p38δ‐unique H30. This work reveals how inhibitor selectivity is achieved by deliberate remodeling of the drug binding site leveraging structural features outside the binding site commonly overlooked in structure‐guided design.

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Publication Details

Journal
Angewandte Chemie International Edition
Published
2026-09-15
DOI
https://doi.org/10.1002/anie.2953141
Primary Topic
Melanoma and MAPK Pathways
Type
article
Field-Weighted Citation Impact
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article

Thinking Outside the Binding Site: A Self‐Encapsulating Kinase Inhibitor Remodels Its Pocket to Achieve Selectivity

Ramona Rudalska, David E. Heppner, Tahereh Damghani, Stefan Laufer et al.
Angewandte Chemie International Edition
Melanoma and MAPK Pathways
article

Thinking Outside the Binding Site: A Self‐Encapsulating Kinase Inhibitor Remodels Its Pocket to Achieve Selectivity

Ramona Rudalska, David E. Heppner, Tahereh Damghani, Stefan Laufer, Ekaterina Hermann, Monica R. MacDonald, Lars Zender, Nader N. Nasief, Daniel Dauch, Nico J. Seidler, Michael Förster, Yuliia Skliarenko, Sahba Cunningham, Kaly S. Lin, Tess M. Weber, Lorenz Mayer, Mareike B. Möllers, Athina A. Moschopoulou, Marcia I. Goettert, Abid N. Manzar, Frederik W. Hacker
article en

Abstract

ABSTRACT Rendering kinase inhibitors selective is a strict requirement in drug development and remains a persistent challenge. To identify new routes to engineer selectivity, we have discovered a first‐in‐class p38δ‐isoform selective inhibitor reflecting 12 000‐fold selectivity improvement over currently available compounds and superior kinome targeting. X‐ray crystallographic characterization indicates that these molecules bind through noncanonical n–π–π stacking sandwich interactions enabled by structural remodeling of the P‐loop. Structural and functional analysis indicates that these selective inhibitors are self‐encapsulating agents due to direct steric clashing that occludes the binding site in a conformation reinforced by a hydrogen‐bonding network involving p38δ‐unique H30. This work reveals how inhibitor selectivity is achieved by deliberate remodeling of the drug binding site leveraging structural features outside the binding site commonly overlooked in structure‐guided design.

Angewandte Chemie International Edition
Buffalo State University (US), Roswell Park Comprehensive Cancer Center (US), Heidelberg University (DE), Universitätsklinikum Tübingen (DE), National Center for Tumor Diseases (DE), University Children's Hospital Tübingen (DE), Bernstein Center for Computational Neuroscience Tübingen (DE), Jacobs Institute (US), University at Buffalo, State University of New York (US), University of Tübingen (DE)
Good health and well-being
Openalex Percentile: Top 18%
Melanoma and MAPK Pathways
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