Targeting Cancer with Precision
Dr. Nayiar Shahid - 10 February 2026
Co-First Author, Alex Kennedy
Cancer treatment faces a long-standing challenge: how to destroy tumor cells without harming surrounding healthy tissue. A new study by Dr. LaPointe’s research group, reported in Bioorganic Chemistry, explores an emerging approach that combines targeted drug design precisely with highly targeted radiation delivery.
The team focused on a protein, called Hsp90 (Heat Shock Protein 90). Inside cells, it acts like a support system, ensuring other proteins in the cell form correctly and remain stable under stress. Cancer cells rely heavily on this process to maintain proper production of proteins involved in the development and maintenance of tumours - including resisting both the immune system and treatments.
Because of this, Hsp90 is a major target for cancer therapy. Several Hsp90‑blocking drugs have reached clinical trials, but none are currently approved for routine use. One major reason is that inhibiting Hsp90 also affects healthy cells, leading to side effects that restrict clinical benefit.
Rather than developing another conventional inhibitor, LaPointe’s team, led by co-first authors, Alexandra Kennedy and Miguel Angel Herrera-Rueda took a different approach. They designed a new class of molecules capable of performing two tasks at once:
- Binding selectively to Hsp90, interfering with its cancer-supporting activity
- Delivering a tiny, highly localized dose of radiation directly to tumor cells
Both tasks are currently being investigated in clinical trials independently but this approach could quite literally kill two birds with one stone. What makes this approach even more desirable is the potential use of the chemical in what is known as radiotheragnostics. In this procedure, the tumour and the compound are visualized using positron emission tomography (PET), and the radioactive signal allows doctors to see whether the compound is reaching the tumor. This could increase the precision of therapy and increase the chances for survival.
In the study, the researchers tested several newly designed molecules based on previously developed Hsp90 inhibitors. These compounds were modified so they could carry a radioactive component, using either bromine or iodine, while still binding tightly to Hsp90. Using computer modeling and laboratory experiments, they identified a number of standout candidates. But only one - known simply as Compound 21 - performed both tasks effectively. For those wondering, bromine was the better option.
While this result represents an important milestone, it is only an early step. So far, the work has been conducted using purified proteins, computer simulations, and cultured cancer cells. Further studies in animal models, followed by clinical trials, will be required to assess safety, effectiveness, and behavior in living systems.
By combining molecular targeting with ultra-localized radiation, this approach could be especially valuable for aggressive or treatment-resistant cancers that rely heavily on Hsp90.
Rather than flooding the body with radiation or broadly toxic drugs, this strategy aims to turn a cancer survival protein into a precise point of attack.