A nanomechanical interface to rapid single-molecule interactions

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Single-molecule techniques provide opportunities for molecularly precise imaging, manipulation, assembly and biophysical studies. Owing to the kinetics of bond rupture processes, rapid single-molecule measurements can reveal novel bond rupture mechanisms, probe single-molecule events with short lifetimes and enhance the interaction forces supplied by single molecules. Rapid measurements will also increase throughput necessary for technological use of single-molecule techniques. Here we report a nanomechanical sensor that allows single-molecule force spectroscopy on the previously unexplored microsecond timescale. We probed bond lifetimes around 5 μs and observed significant enhancements in molecular interaction forces. Our loading-rate-dependent measurements provide experimental evidence for an additional energy barrier in the biotin-streptavidin complex. We also demonstrate quantitative mapping of rapid single-molecule interactions with high spatial resolution. This nanomechanical interface may allow studies of molecular processes with short lifetimes and development of novel biological imaging, single-molecule manipulation and assembly technologies.
Original languageEnglish
JournalNature Communications
Pages (from-to)247
Publication statusPublished - 2011

    Research areas

  • Bacterial Proteins, Biotin, Kinetics, Mechanics, Microscopy, Atomic Force, Molecular Imaging, Nanotechnology, Spectrum Analysis, Streptavidin, Thermodynamics

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