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

[Image: see text] 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...

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Autores principales: Matsushita, Takahiko, Maruyama, Naoto, Koyama, Tetsuo, Hatano, Ken, Matsuoka, Koji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9520716/
https://www.ncbi.nlm.nih.gov/pubmed/36188280
http://dx.doi.org/10.1021/acsomega.2c04379
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author Matsushita, Takahiko
Maruyama, Naoto
Koyama, Tetsuo
Hatano, Ken
Matsuoka, Koji
author_facet Matsushita, Takahiko
Maruyama, Naoto
Koyama, Tetsuo
Hatano, Ken
Matsuoka, Koji
author_sort Matsushita, Takahiko
collection PubMed
description [Image: see text] 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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spelling pubmed-95207162022-09-30 Modification of Fab Fragments by Dibromopyridazinediones Carrying Mono- and Double-Biotin Functionalities Matsushita, Takahiko Maruyama, Naoto Koyama, Tetsuo Hatano, Ken Matsuoka, Koji ACS Omega [Image: see text] 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. American Chemical Society 2022-09-14 /pmc/articles/PMC9520716/ /pubmed/36188280 http://dx.doi.org/10.1021/acsomega.2c04379 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Matsushita, Takahiko
Maruyama, Naoto
Koyama, Tetsuo
Hatano, Ken
Matsuoka, Koji
Modification of Fab Fragments by Dibromopyridazinediones Carrying Mono- and Double-Biotin Functionalities
title Modification of Fab Fragments by Dibromopyridazinediones Carrying Mono- and Double-Biotin Functionalities
title_full Modification of Fab Fragments by Dibromopyridazinediones Carrying Mono- and Double-Biotin Functionalities
title_fullStr Modification of Fab Fragments by Dibromopyridazinediones Carrying Mono- and Double-Biotin Functionalities
title_full_unstemmed Modification of Fab Fragments by Dibromopyridazinediones Carrying Mono- and Double-Biotin Functionalities
title_short Modification of Fab Fragments by Dibromopyridazinediones Carrying Mono- and Double-Biotin Functionalities
title_sort modification of fab fragments by dibromopyridazinediones carrying mono- and double-biotin functionalities
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9520716/
https://www.ncbi.nlm.nih.gov/pubmed/36188280
http://dx.doi.org/10.1021/acsomega.2c04379
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