This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Across every cell in the body, molecules are constantly pulling, gripping and releasing under mechanical strain. That force often decides whether a drug sticks to its target, whether a cell holds its shape or whether a disease takes hold.
The problem is that almost nobody is measuring that molecular tug-of-war, UBC Okanagan researcher Dr. In a study published in the journal Science Advances, a team of chemists describes a new way to close that gap. "Force is an important variable in many biological interactions, but it is not routinely measured in standard binding assays," says Li, a chemistry researcher and the study's senior author.
"We wanted to develop a method that makes force measurements parallel and accessible." The method, called tether force spectroscopy, applies precisely controlled forces to hundreds of individual molecules at the same time and watches how each one responds. It's a combination of scale, precision and affordability that existing tools have struggled to deliver together. The researchers validated it against the field's gold-standard instrument, then used it to measure molecules being stretched, unzipped and pulled apart at forces spanning the full range relevant to biology.
They have filed a patent on the approach and are exploring how to turn it into a commercial product. Standard lab tests can tell you if two molecules bind in a test tube, but these tests don't account for the forces that molecules experience in our bodies. To better understand how these molecules will behave in the dynamic environments of our cells, scientists use equipment to pull molecules apart with precisely controlled forces and measure how they respond.
While this approach is powerful, it comes with challenges that limit its use to a very small number of highly specialized labs. Many of these challenges stem from the need to attach molecules to microscopic objects like beads to grab hold of them and pull. These beads add variability, skew results and complicate experiments, while often limiting measurements and requiring expensive equipment to control.
Tether force spectroscopy is a workaround that replaces those beads with a long strand of DNA tethered to a target molecule, then runs a current of fluid past it. The DNA catches the flow like a sail, and the stronger the current, the harder the sail tugs on the molecule anchored below. By tagging both the sail and the target so they glow, researchers can watch in real time how a molecule stretches, shifts or comes apart in response to precisely controlled forces.
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