Watching Cancer Proteins in Real Time, with Help from Rare Earth Elements
Researchers from the Broad Institute and MIT have developed a new single-molecule imaging platform using rare earth element-doped probes to observe cancer proteins in real time. The study revealed that HER3 homodimers are more stable than previously thought, providing new insights for cancer therapy development.
Why it matters
This advancement in imaging technology allows for longer, more detailed observation of protein behavior, which could lead to more effective targeted cancer treatments.
A long-duration single-molecule imaging platform from the Broad Institute and MIT has revealed unexpected stability in homodimers of HER3, one of the most enigmatic members of the ErbB receptor family. The research, published in Cell , shows wild-type HER3 forms unexpectedly stable homodimers, and that cancer mutations destabilize these homodimers. The findings could hopefully help shape new cancer therapies. Their paper is entitled, “ ErbB family receptor dimerization dynamics and dysregulation via long-term single-molecule imaging .”
But the tool that delivered it matters just as much: an upconverting nanoparticle (UCNP) probe, doped with heavy rare earth elements, that simply doesn’t photobleach.
In one corner of Sam Peng’s lab, the imaging rig looks almost improvised. Cameras, lenses, and lasers are bolted directly onto a metal breadboard, like an enormous sheet of Legos built by hand rather than bought off a shelf.
Get smarter about the news
Sign up free for a feed built around what you actually care about, Dive Deeper research on any story, and the full text of every article.
Create free accountAlready have an account? Sign in