Authors
Shoji Kashiwabara, Md Sifat Islam, Makusu Tsutsui, Masateru Taniguchi
Published in
ACS sensors. Jul 21, 2026. Epub Jul 21, 2026.
Abstract
Proteins derive their biological identity from an amino acid sequence, and even subtle sequence variations can mark disease states, therapeutic response, and cancer progression. Although solid-state nanopores offer single-molecule sensitivity, protein analysis with conventional nanopores remains limited by stochastic capture, rapid translocation, and the need for sub-nanometer control over pore dimensions. Here, we report that this size-matching requirement can be bypassed by converting sequence-dependent protein surface chemistry into amplified particle-scale transport signatures through leveraging chaotropic chemistry for surface charge modulation. We immobilized monoclonal anti-prostate-specific antigen antibody variants, differing only in partial amino acid sequence, on polymeric microparticles and measured their passage through readily fabricated SiNx micropores. In the presence of guanidine hydrochloride, chaotropic perturbation of hydration shells and compression of the electric double layer reshaped the electrokinetic landscape around the particle-protein complexes in a variant-dependent manner. These chemically amplified differences generated distinct resistive pulse waveforms, allowing near-perfect discrimination of antibody variants by machine learning. This approach shifts protein sensing from geometrical confinement in nanoscale pores to chemically tuned amplification in micrometer-scale pores, providing a scalable route to sequence-sensitive biomarker profiling without advanced nanofabrication.
PMID:
42479543
Bibliographic data and abstract were imported from PubMed on 22 Jul 2026.
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