The University of Texas MD Anderson Cancer Center has signed a new collaboration agreement with Amorfix Life Sciences in which antibodies thought to help direct cancer treatments will be used by the center to identify misfolded proteins, which are incorrectly created protein cells that are part of the development of lung cancer.
Misfolded proteins are cells in which the amino acids are not aptly folded into a fully functional three dimensional protein. They form a mutated aggregate that is harmful to the body and is thought to cause disease.
Several diseases that share no other similarities have all been found to contain pockets of misfolded proteins. These diseases include diabetes, cancer, Alzheimer’s, and Huntington’s disease.
Amorfix Life Sciences Ltd. is on the forefront of developing diagnostic systems that target diseases with misfolded proteins. They already have three proprietary methods for identifying misfolded proteins in tissue samples. Two of them are Epitope Protection™ and AMFIA™. They have allowed the creation of a screening test to predict Alzheimer’s disease as well as mild cognitive impairment.
The other system they use is called ProMIS™. It is a computer-based algorithm that tracks Disease Specific Epitopes (DSEs) and can help with the discovery and diagnosis of many diseases that share the misfolded proteins. With the help of the ProMIS™ system, the DSE’s that mark a particular cell structure as misfolded allow for the creation of antibodies that only target the areas of misfolded proteins while ignoring healthy cells. This permits antibody treatment that will attack the diseased cells found in tumors while not damaging the surrounding healthy tissue and organ cells.
“This collaboration agreement with MD Anderson will enable more rapid translation of Amorfix discoveries to the patients in need of them,” said the Founder and Chief Scientific Officer of Amorfix, Dr. Neil Cashman.
The Cancer Center will be trying to find misfolded proteins on the surface of lung cancer tumors and then find ways of creating antibodies that will bind to those cells creating targeted therapeutic intervention that is not as damaging to the overall health of the patient. The ideal outcome would be using the internal structure of misfolded proteins to create treatments that do not rely on the wide-scale cellular damage that is associated with chemotherapy and radiation.