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G-quadruplexes are specialized DNA and RNA structures that form in guanine-rich regions critical for telomere integrity and cellular aging. These dynamic structures regulate gene expression and chromosome stability, with disruption implicated in cancer development and aging-related diseases. Despite extensive study, scientists cannot directly observe how G-quadruplexes fold and function in real biological contexts—limiting our ability to target them therapeutically. With cancer affecting millions worldwide, understanding these structures has become essential for developing novel targeted treatments.
Case study
A study led by Bo Sun at ShanghaiTech University explored how human telomerase RNA (hTR) forms and maintains stable G-quadruplex structures. Using LUMICKS C-Trap, they monitored real-time folding and unfolding of single hTR molecules, revealing:
Reference:
Ye et al., The Journal of Physical Chemistry Letters (2021).
Prof. Bo Sun Lab - ShanghaiTech University
“Proximal Single-Stranded RNA Destabilizes Human Telomerase RNA G‑Quadruplex and Induces Its Distinct Conformers.”
Expanded repeat sequences in RNA form abnormal structures linked to numerous neurodegenerative diseases including Huntington's, ALS, and certain ataxias. These toxic RNA structures aggregate in cells and disrupt normal neuronal function, triggering progressive neurodegeneration. Despite significant advances in genetic diagnosis, researchers cannot visualize how these repeat expansions actually misfold and aggregate —hampering therapeutic development. With neurodegenerative disorders affecting over 50 million people globally, understanding RNA structural dynamics has become critical for developing effective treatments.
Case study
Researchers Christian Kaiser and Sarah Woodson at Johns Hopkins University investigated how expanded CAG repeats in HTT mRNA influence misfolding and aggregation. By applying real-time single-molecule force measurements with LUMICKS C-Trap, they discovered:
Reference:
O’Brien et al., Nature Communications (2024).Prof. Christian Kaiser and Prof. Sarah Woodson - Johns Hopkins University“Stick-slip unfolding favors self-association of expanded HTT mRNA.”
RNA pseudoknots are complex folded structures that regulate critical processes in viral replication and gene expression. These dynamic elements enable viruses to produce multiple proteins from limited genetic material and evade host defenses through conformational changes. Despite their central role in viral pathogenesis, scientists cannot directly observe how these structures interact with host proteins during infection—limiting antiviral development. With viral diseases continuously threatening global health security, understanding RNA structural dynamics has become essential for creating next-generation antivirals.
Case study
A study led by the Neva Caliskan Lab at the Helmholtz Institute for RNA-Based Infection Research investigated how ZAP-S protein modulates SARS-CoV-2 frameshifting through altering the pseudoknot structure. By directly tracking the real-time pseudoknot structural dynamics in the presence or absence of ZAP-S using LUMICKS C-Trap, they revealed:
Reference:
Zimmer et al., Nature Communications (2021).Prof. Neva Caliskan - Helmholtz Institute for RNA-Based Infection Research“The short isoform of the host antiviral protein ZAP acts as an inhibitor of SARS-CoV-2 programmed ribosomal frameshifting.”
Bacterial integrons are genetic elements that enable bacteria to capture external genes and develop antibiotic resistance. These molecular machines incorporate resistance genes through DNA recombination, driving the spread of untreatable infections. Despite decades of research, scientists still cannot explain why some genes transfer efficiently while others don't—a critical gap hindering our ability to predict resistance spread. With resistant infections causing over 1.2 million deaths annually, understanding these mechanisms has become urgent.
Case study
A breakthrough study led by Michael Schlierf at TU Dresden in collaboration with Didier Mazel at Institut Pasteur investigated this mystery using single-molecule techniques. By applying controlled forces to individual DNA-IntI1 integrase complexes with LUMICKS C-Trap, they revealed:
Reference: Vorobevskaia et al., Science Advances (2024). Prof. Michael Schlierf Lab - TU Dresden & Prof. Didier Mazel Lab - Institut Pasteur "The recombination efficiency of the bacterial integron depends on the mechanical stability of the synaptic complex."
The C-Trap® provides the world’s first dynamic single-molecule microscope to allow simultaneous manipulation and visualization of single-molecule interactions in real time.