Three molecules of the statin atorvastatin can wedge into a single pocket on a calcium channel in muscle cells and hold it open, according to a structural study led by University of British Columbia biochemists. Postdoctoral researcher Steven Molinarolo and senior author Filip Van Petegem used cryo-electron microscopy to map the contact, and the finding offers a candidate explanation for the soreness and weakness that lead some patients to quit the drug. ScienceDaily carried a write-up of the work on Oct. 20, 2026.
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The result is a mechanism, not a clinical verdict. The experiments were done on purified protein structures rather than on patients, and the authors frame the calcium leak as a likely driver of muscle symptoms that still needs further testing. That distinction matters for the roughly 200 million people worldwide who take a statin, most of whom never develop serious muscle trouble.
Three atorvastatin molecules in one RyR1 pocket
The channel at the center of the study is ryanodine receptor 1, abbreviated RyR1, a protein that controls how calcium is released inside skeletal muscle cells during contraction. In a healthy fiber the release is brief and tightly regulated. What the UBC team saw was a sequence: the first statin molecule attaches while the channel is closed and makes opening more likely, and the second and third then hold the channel open so that calcium keeps leaking into places where it should be tightly controlled.
The group reported its structures in Nature Communications, in a paper titled “Cryo-electron microscopy reveals sequential binding and activation of Ryanodine Receptors by statin triplets.” Carmen Valdivia and Héctor Valdivia are the other two authors named in the journal reference, and the imaging was carried out at UBC’s high-resolution macromolecular cryo-electron microscopy facility. Molinarolo said the images let the team see, almost atom by atom, how statins latch onto the channel, which is what makes the three-step sequence credible rather than inferred from indirect biochemical assays alone. The journal page is also available at nature.com.
What the calcium leak could mean for sore muscles
Molinarolo drew a direct line from structure to symptoms in the university’s announcement of the study: “That leak of calcium explains why some patients experience muscle pain or, in extreme cases, life-threatening complications.” Van Petegem described the images as the first clear picture of how statins activate this channel. The authors propose that a continuous leak of this kind can damage muscle tissue, which is why the pocket is a plausible suspect, though they stop short of declaring it the only route to statin muscle problems, and the paper does not follow individual patients from drug exposure to symptoms.
Severe muscle injury strikes only a small fraction of statin users, while milder soreness, weakness and fatigue are more common and can push people off a drug that protects the heart. Neither the university release nor the ScienceDaily summary gives a percentage of patients affected, so no figure is offered here. Because the structural result cannot say how often the leak occurs in a living patient, or what dose or duration it takes to matter, the number of people who might benefit from a redesigned statin is not something this research can estimate.
Only one statin was studied, and drug design is next
The structures were solved with atorvastatin, one of several widely prescribed statins. The UBC team suggests the interaction may be common across the class, but the work did not test the other statins in detail, so whether simvastatin, rosuvastatin or others occupy the same pocket in the same way remains to be shown. The study also contains no trial data, and the authors use conditional language about what the structure could guide.
Van Petegem sees the practical payoff in chemistry. He called the structure a roadmap for designing statins that do not interact with muscle tissue, and the university release quotes him saying that statins have been a cornerstone of cardiovascular care for decades. If the muscle-binding portion of the molecule can be separated from the part that lowers cholesterol, a redesigned drug could in principle keep the benefit while cutting the risk.
A timing note for readers who see this story circulating again: the paper and the UBC release date from late 2025, with the university announcement posted Nov. 26, 2025, and the ScienceDaily write-up appeared in October 2026. Nothing in either source suggests the findings have since been revised or overturned, and no new statin has yet been developed from them.
For now, patients with muscle pain on a statin have no new test or treatment arising from this research. Any change to a prescription is a decision for a clinician, and the study’s contribution is to give drug designers a specific atomic target to work from.
Van Petegem said the aim is to make statins even safer, so that patients can benefit without fear of serious side effects. Neither source describes a candidate compound yet.
This article was produced with the assistance of AI and reviewed by Morning Overview editors prior to publication.
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