Natriuretic peptides can relieve cardiovascular stress and closely related to
heart failure. Besides, these
peptides also have preferable interactions of binding to cellular
protein receptors, and subsequently mediate various physiology actions. Hence, detection of these circulating
biomarkers could be evaluated as a predictor ("Gold standard") for rapid, early diagnosis and risk stratification in
heart failure. Herein, we proposed a measurement to discriminate multiple
natriuretic peptides via the
peptide-
protein nanopore interaction. The nanopore single-molecular kinetics revealed that the strength of
peptide-
protein interactions was in the order of ANP > CNP > BNP, which was demonstrated by the simulated
peptide structures using SWISS-MODEL. More importantly, the
peptide-
protein interaction analyzing also allowed us to measure the
peptide linear analogs and structure damage in
peptide by single-chemical bond breakup. Finally, we presented an ultra-sensitive detection of plasma
natriuretic peptide using asymmetric
electrolyte assay, obtaining a detection limit of ∼770 fM for BNP. At approximately, it is 1597 times lower than that of using symmetric assay (∼1.23 nM), 8 times lower than normal human level (∼6 pM), and 13 times lower than the diagnostic values (∼10.09 pM) complied in the guideline of European Society of Cardiology. That said, the designed nanopore sensor is benefit for
natriuretic peptides measurement at single molecule level and demonstrates its potential for
heart failure diagnosis.