Dresden 2026 – scientific programme
Parts | Days | Selection | Search | Updates | Downloads | Help
BP: Fachverband Biologische Physik
BP 14: Poster Session II
BP 14.81: Poster
Tuesday, March 10, 2026, 18:00–21:00, P2
Pulling Geometry as a Design Parameter for Coiled Coil-Based Molecular Force Sensors — •Laura M. Wolfthaler1, Zeynep Atris2, Angelo Valleriani2, Russell J. Wilson1,2, and Kerstin G. Blank1,2 — 1Johannes Kepler Universität, Linz, Austria — 2Max Planck Institute of Colloids and Interfaces, Potsdam, Germany
Molecular force sensors (MFSs) measure piconewton-scale forces central to cell adhesion, migration and differentiation. While DNA-based MFSs are well established, their functionalization requires multistep chemistry. We introduce a protein-based MFS building block derived from heterodimeric coiled coils (CCs). Building on our prior work showing how CC length, helix stability and core packing shape mechanics, we now identify pulling geometry as a powerful and versatile parameter for tuning CC mechanical stability without altering thermodynamic or kinetic properties. Using atomic force microscope-based single-molecule force spectroscopy, we applied force parallel and perpendicular to the CC superhelix and observed strongly geometry-dependent rupture forces, including distinct responses for the two shear modes of a 4-heptad heterodimer. These results highlight how local helix stability and structural anisotropy determine CC mechanical behavior. This work establishes a foundation for using MFSs across a wide range of cell culture applications. Their ability to report forces at molecular scales could transform how mechanical signaling is studied at cell-material interfaces.
Keywords: single molecule force spectroscopy; molecular force sensors; coiled coil; protein mechanics