A New Process Urges Cancerous Cells To Consume Toxic Drugs

Researchers at the Massachusetts General Hospital (MGH) have recently carried out a vital study that leads to the enhanced absorption of anticancer drugs by the tumor cells. This would help in significantly boosting the effectiveness of chemotherapy treatment. The results of this study are published in the journal Nature Nanotechnology. The key challenge being faced by medical professionals in treating the tumor is to deliver the desired dosage of anticancer drugs to the affected tissues in the body. To overwhelm this challenge, the basic strategy is employed to enclose the medications inside the albumin, a protein present in ample amounts in the blood. According to the researchers, the tumor cells ingest food in the form of proteins and nutrients for constant multiplication. The anticancer drugs adhered to the albumin proteins also penetrate inside the tumor cells, which leads to the destruction of nasty cells.

The U.S. Food and Drug Administration has approved an albumin-bound drug nanoparticle called albumin-bound paclitaxel (nab-PTX), which is extensively used in the country for treating pancreatic cancer and severe lung cancer. Miles Miller, principal investigator and the senior author of the study, stated that each volunteer responded differently to the nab-PTX drug and their opinion regarding the drug delivery effectiveness was mixed. Moreover, the study involved an incompetent material that not only affects anticancer drug delivery but also has some side effects.

Miller along with his team of researchers at the MGH comprehensively accessed the delivery of nab-PTX using a cancer cell model in the mouse. They employed several sophisticated techniques such as 3D microscopy and tissue clearing methods throughout the research. They discovered that a certain amount of nab-PTX adhered to albumin protein was absorbed by the tumor cells. In addition, the rate of absorption of anticancer drugs by tumor cells can be controlled by certain cell-signaling pathways associated with albumin protein.