Auburn University researchers, in collaboration with the University of Basel, have made significant strides in improving the stability of cancer-targeting protein complexes. This advancement could pave the way for more effective and precise cancer treatments with reduced side effects.
The study, published in ACS Nano, focuses on the interaction between PD-L1, a protein used by tumors to evade the immune system, and Affibodies, small proteins designed to bind to cancer cells and deliver therapeutic agents. By investigating the concept of "force anisotropy," the team discovered that adjusting attachment points between PD-L1 and Affibodies could significantly increase the strength of their bond.
Rafael Bernardi, co-senior author on the paper, explained, "By adjusting where we attach Affibodies, we can make them stronger so they stay intact in the body longer, helping them reach cancer cells more effectively."
The researchers found that these adjustments could make the protein complex up to four times stronger and even more stable under tension.
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This breakthrough has important implications for drug delivery systems in cancer treatment. By creating more stable protein complexes, researchers can develop therapies that target tumors more precisely and remain effective for longer periods. The enhanced stability could also improve the effectiveness of Affibodies in cancer surgery, where they can be used to make tumors more visible or deliver targeted radiation therapy.
Moving forward, the team is working on designing even stronger Affibody proteins capable of targeting various cancer types with greater accuracy.