Modification of Fab Fragments by Dibromopyridazinediones Carrying Mono- and Double-Biotin Functionalities

Overview

Journal ACS Omega

Publisher American Chemical Society

Specialty Chemistry

Date 2022 Oct 3

PMID 36188280

Authors

Takahiko Matsushita

Naoto Maruyama

Tetsuo Koyama

Ken Hatano

Koji Matsuoka

Affiliations

Soon will be listed here.

Abstract

To verify the potencies of dibromopyridazinediones with mono- and double-biotin groups, the functions as cysteine-selective biotinylation reagents were evaluated through conjugation with a goat anti-mouse IgG Fab fragment as a functional protein model. The starting Fab was reduced with tris(2-carboxyethyl)phosphine to cleave the disulfide bond and then treated with the reagents. These reagents simultaneously introduced biotin groups into the reduced Fab and re-bridged the disulfide moiety. Furthermore, we demonstrated that the biotin-labeled Fabs were reactive to an antigen and streptavidin.

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