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BP: Fachverband Biologische Physik
BP 27: Single Molecule Biophysics
BP 27.11: Talk
Thursday, March 21, 2024, 12:30–12:45, H 0112
Structure-Mechanics Relationships of Heterodimeric Coiled Coils — Zeynep Atris1, Anna-Maria Tsirigoni1, Melis Goktas1, Patricia Lopez Garcia1, Russell J. Wilson1,2, Angelo Valleriani1, Ana Vila Verde3, and •Kerstin G. Blank1,2 — 1Max Planck Institute of Colloids and Interfaces, Potsdam, Germany — 2Johannes Kepler University, Linz, Austria — 3University of Duisburg-Essen, Duisburg, Germany
Coiled coil (CC) structural motifs are found in diverse array of different proteins. Consisting of self-assembled alpha-helices that create helical superstructures, they serve as key elements of cytoskeletal and extracellular matrix proteins. Despite their widespread occurrence as mechanical building blocks, the fundamental structural factors governing their molecular mechanical properties have remained largely elusive.
We are applying AFM-based single molecule force spectroscopy and steered molecular dynamics simulations to determine the structure-to-mechanics relationship of de novo designed, synthetic CCs. When comparing heterodimeric CCs of varying length and sequence, our findings reveal that higher thermodynamic and kinetic stability does not always correlate with higher rupture forces within the range of AFM-accessible loading rates. We further observe that a single sequence can exhibit diverse mechanical stabilities under different loading geometries. This knowledge is now utilized for the development of a library of CC-based mechanoresponsive hydrogel crosslinks for tissue engineering applications.
Keywords: single-molecule force spectroscopy; protein mechanics; AFM; molecular dynamics simulations