Fig. 4: Sensitivity for single amino acid variation-induced changes in volume or conformation.
From: Nanopore sensing of protein and peptide conformation for point-of-care applications
a Schematic representation of the characterization of peptides with different types of amino acid mutations such as deletion, addition, or substitution by a nanopore. b Identification and discrimination of sequential C-terminal deletion of angiotensin by the enzyme ACE and/or ACE2 (angiotensin-converting enzyme) with an aerolysin nanopore, as defined by the distribution of dwell time (ms) against the mean blockade level (I/I0) in 1 M KCl, 10 mM Tris, 1 mM EDTA, pH 8. Figure adapted from Nature Chem., Jiang et al.123. c Current traces showing the discrimination between Endothelin 1 and 2 in a mixture with a FraC nanopore in 1 M KCl, 0,1 M citric acid, 180 mM Tris, pH 4,5. Figure adapted from Nature Com., Huang et al.124. d Discrimination of Bradykinin (BK) and Des-Arginine bradykinin (Des-Arg BK) and identification of different conformations in serum (2%) identified with Principal Component Analysis and machine learning with an aerolysin nanopore in 4 M KCl, 25 mM Tris, pH 7,5. Reprinted (adapted) with permission from Greive, et al. Identification of Conformational Variants for Bradykinin Biomarker Peptides from a Biofluid Using a Nanopore and Machine Learning. ACS Nano 18, 539–550 (2024). Copyright 2024, American Chemical Society119. Created in BioRender. Ratinho, L. (2025) https://BioRender.com/t96d726.
