UCLA researchers have developed a method to use TGF-beta binding peptides such as BBP to bind TGF-beta and remove it from solution for treatment of metastatic diseases.
Metastatic cancer is a cancer that can spread from the part of the body where it started to other parts of the body, which makes them harder to treat. Therefore, there is a need for more effective and less toxic therapeutics to manage metastatic diseases. The transforming growth factor beta (TGF-beta) signaling pathway is a key player in metastatic diseases and its misregulation can result in tumor development. The TGF-beta superfamily is comprised of over 40 members, including TGF-betas and bone morphogenetic proteins (BMPs).
Previous studies have shown that neutralizing TGF-beta with antibodies improves outcomes in animal models of metastatic diseases. Bone morphogenetic proteins (BMPs) are a group of growth factors that are able to induce the formation of bone and cartilage. The inventors had previously discovered that BMP binding peptides (BBPs) bind to BMP-2 and inhibit BMP-2 activity in vitro. The parental protein of BBP, spp24, binds BMP-2 in vivo and inhibits its activity, and it is known that BBP binds to TGF-beta as well.
UCLA researchers have developed a method to use TGF-beta binding peptides such as BBP to bind TGF-beta and remove it from solution for treatment of metastatic diseases. TGF-beta binding peptides would be delivered to the site of metastases to neutralize TGF-beta and BMPs.
UCLA researchers have demonstrated the binding of TGF-beta to BBP.