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Although in situ atomic force microscopy (AFM) can allow single‐molecule detection of antibody–antigen binding, the practical applications of in situ AFM for disease diagnosis are greatly limited, due to its operational complexity and long operational times, including the execution time for the surface chemical/biological treatments in the equipped glass liquid cell. In this report, we present a method of graphically superimposed alignment that enables ex situ AFM analysis of an immobilized antibody at the same location on a semiconductor chip surface before and after incubation with its antigen. All of the required chemical/biological treatments can be executed feasibly using standard laboratory containers, allowing single‐molecule ex situ AFM detection to be performed with great practicality, flexibility, and versatility. As an example, we describe the analysis of hepatitis B virus X protein (HBx) and its IgG antibody. Using ex situ AFM, we extracted individual information about the topographical characteristics of the immobilized single and aggregated IgG antibodies on the chip surface and analyzed the data statistically. Furthermore, we investigated, in a statistical manner, the changes in AFM‐measured heights of the individual and aggregated IgG antibodies that occurred as a result of changes in conformation upon formation of IgG–HBx complexes. This article is protected by copyright. All rights reserved.
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Single‐Molecule Ex Situ Atomic Force Microscopy Allows Detection of Individual Antibody–Antigen Interactions on a Semiconductor Chip Surface
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