Rxivist logo

Designed Anchoring Geometries Determine Lifetimes of Biotin-Streptavidin Bonds under Constant Load and Enable Ultra-Stable Coupling

By Sophia Gruber, Achim Löf, Steffen M. Sedlak, Martin Benoit, Hermann E. Gaub, Jan Lipfert

Posted 14 May 2020
bioRxiv DOI: 10.1101/2020.05.12.090639

The small molecule biotin and the homotetrameric protein streptavidin (SA) form a stable and robust complex that plays a pivotal role in many biotechnological and medical applications. In particular, the biotin-streptavidin linkage is frequently used in single molecule force spectroscopy (SMFS) experiments. Recent data suggest that biotin-streptavidin bonds show strong directional dependence and a broad range of multi-exponential lifetimes under load. Here, we investigate engineered SA variants with different valencies and a unique tethering point under constant forces using a magnetic tweezer assay. We observed two orders-of-magnitude differences in the lifetimes, which we attribute to the distinct force loading geometries in the different SA variants. We identified an especially long-lived tethering geometry that will facilitate ultra-stable SMFS experiments and pave the way for new biotechnological applications. ### Competing Interest Statement The authors have declared no competing interest.

Download data

  • Downloaded 182 times
  • Download rankings, all-time:
    • Site-wide: 71,635 out of 88,669
    • In biophysics: 3,114 out of 3,853
  • Year to date:
    • Site-wide: 17,633 out of 88,669
  • Since beginning of last month:
    • Site-wide: 18,129 out of 88,669

Altmetric data

Downloads over time

Distribution of downloads per paper, site-wide


Sign up for the Rxivist weekly newsletter! (Click here for more details.)