Immunoactivity of Self-assembled Antibodies Investigated by Atomic Force Microscopy

Overview

Journal RSC Adv

Publisher Royal Society of Chemistry

Specialty Chemistry

Date 2022 May 13

PMID 35547980

Authors

Hiroaki Kominami

Kei Kobayashi

Shinichiro Ido

Hirokazu Kimiya

Hirofumi Yamada

Affiliations

Soon will be listed here.

Abstract

Immunoglobulin G (IgG), an antibody, plays a significant role in the immune system, and the functions of IgG molecules have been studied in many research fields such as medicine and engineering. Recently, we found the self-assembly of monoclonal mouse IgG molecules on a mica substrate using atomic force microscopy (AFM); the IgG molecules self-assemble into hexamers and the hexamers form a two-dimensional (2D) crystal. The self-assembly of the IgG molecules is of great interest in terms of the enhancement of the immunoactivity of the antibodies. In this study, we investigated the self-assembly of various IgG molecules on a mica substrate to discuss if the hexamerization of the IgG molecules is a general phenomenon. We also investigated the antigen binding site in the IgG antibody hexamers, and estimated the association rate constant of the self-assembled IgG molecules based on the AFM measurements. The estimated value was lower than that reported in a previous study probably because of the limited mobility of the antigen-binding fragments on the substrate.

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