Snapshots from all-atom MD simulations tentatively indicate that non-specific interactions of the polyadenine oligos with the SiNx surfaces are responsible for the extended protein linker–oligo translocation dwell times in the ssNPs.
A technology developed in the laboratory of Prof. Amit Meller from the Technion Israel Institute of Technology Faculty of Biomedical Engineering marks a significant advancement toward rapid proteome analysis, with far-reaching implications for both fundamental research and disease diagnosis. Reported in Nature Nanotechnology, the system can map whole proteins and generate a unique electrical “fingerprint” for each molecule.
Led by Prof. Meller and postdoctoral fellow Dr. Neeraj Soni, and in collaboration with scientists from the University of Illinois and Rice University, the team’s approach overcomes limitations of traditional methods, which rely on complex molecular motors or protein-specific antibodies. Their technology uses synthetic nanometer-scale pores and a stick slip mechanism to control protein movement, recording ionic currents as proteins traverse the pore. These signals are decoded to identify proteins quickly and accurately.
The initial study targeted cysteine, found in nearly 97% of human proteins, demonstrating broad applicability. The method is adaptable to other amino acids and post-translational modifications, making it relevant for the entire proteome.
Beyond accelerating protein research, the technology has clinical potential for rapid, cost-effective diagnostics and personalised treatments from simple samples like blood. Prof. Meller envisions a point-of-care platform for hospitals, laboratories, and research centres, offering a transformative approach to protein analysis and healthcare.
Image credit: Nature Nanotechnology (2025). DOI: 10.1038/s41565-025-02016-w (Phys.org)
