New method achieves functional protein delivery into living cells

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In cooperation with researchers from the China University of Petroleum, the working group of Dr. Werner Nau, Professor of Chemistry at Constructor University, has demonstrated the effectiveness of a new method of intracellular protein transport.

The results of their research are published in the Proceedings of the National Academy of Sciences.

"We are the first to succeed in transporting a completely functional protein into living cells without disrupting cellular integrity—simply by adding a small molecule," says Nau. This method could have the potential for the next stage of drug delivery.

Cells are masters of self-defense, protecting themselves with a multitude of barriers. Circumventing them to deliver a therapeutic protein into a cell undamaged is a central goal of research.

While previous methods have mainly relied on the encapsulation of proteins, researchers at Constructor University, on the other hand, utilized boron cluster anions as a molecular transport vehicle, which they use to place a protein called cytochrome C in the cells. Here, it can unfold its toxic activity and eventually induce cell death.

Boron clusters are inorganic, water-soluble compounds that are not degraded by enzymes or bacteria in the body. "They are a highly efficient means of protein transport," says Dr. Andrea Barba-Bon, a young scientist in Nau's research group. The protein remains bioactive in the cell and can carry out its task, such as fighting tumors.

"Intracellular delivery of proteins has the potential to revolutionize cell biology research and medical therapy, with broad applications in bioimaging, disease treatment and genome editing," the study states.

The next step in research is now to make protein transport more targeted in order to combat individual diseases more directly. "But this is a long process," says Barba-Bon.

More information: Xiqi Ma et al, A small-molecule carrier for the intracellular delivery of a membrane-impermeable protein with retained bioactivity, Proceedings of the National Academy of Sciences (2024). DOI: 10.1073/pnas.2407515121

Journal information: Proceedings of the National Academy of Sciences

Provided by Constructor University