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Regensburg 2019 – scientific programme

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BP: Fachverband Biologische Physik

BP 26: Single molecules biophysics

BP 26.2: Talk

Thursday, April 4, 2019, 15:30–15:45, H4

AFM-based Single-Molecule Force Spectroscopy on the Streptavidin:Biotin Interaction — •Steffen M. Sedlak1, Leonard C. Schendel1, Katherine R. Erlich1, Achim Löf1, Rafael C. Bernardi2, Magnus S. Bauer1, Carleen Kluger1, and Hermann E. Gaub11Department of Physics and Center for NanoScience, LMU Munich, Germany — 2University of Illinois at Urbana-Champaign, Urbana, IL, USA

The high-affinity interaction of the small molecule biotin with the tetrameric protein streptavidin (SA) is a widely applied tool for detection, labeling and immobilization of molecules. We study single biotin:SA interactions under force using AFM-based single-molecule force-spectroscopy (SMFS) and steered Molecular Dynamics (sMD) simulations. Probing monovalent SA in various specific tethering geometries, we investigated how the mechanical stability of the biotin:SA interaction depends on the force loading geometry and revealed the underlying molecular mechanism. We made use of the different unbinding forces to realize a protein-based bottom-up nanoscale assembly of single fluorescent molecules by single-molecule cut-and-paste; a unique approach that enables spatially controlled arrangements of diverse molecules into a single ensemble. We also studied SA of different valencies and distinguished unbinding forces of biotin from different SA subunits in AFM-based SMFS. sMD allowed to understand the force-propagation pathways through the SA tetramer. Identifying a long-lived tethering geometry, we can reliably measure single molecules at comparably high constant forces for many hours in magnetic tweezers.

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