Investigation of major amino acid residues of anti-norfloxacin monoclonal antibodies responsible for binding with fluoroquinolones

Abstract It is important to understand the amino acid residues that govern the properties of the binding between antibodies and ligands. We studied the binding of two anti-norfloxacins, anti-nor 132 and anti-nor 155, and the fluoroquinolones norfloxacin, enrofloxacin, ciprofloxacin, and ofloxacin. B...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Patamalai Boonserm, Songchan Puthong, Thanaporn Wichai, Sajee Noitang, Pongsak Khunrae, Sarintip Sooksai, Kittinan Komolpis
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/abc3ebe8a04146e6baa9b970739b961a
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:abc3ebe8a04146e6baa9b970739b961a
record_format	dspace
spelling	oai:doaj.org-article:abc3ebe8a04146e6baa9b970739b961a2021-12-02T15:09:23ZInvestigation of major amino acid residues of anti-norfloxacin monoclonal antibodies responsible for binding with fluoroquinolones10.1038/s41598-021-96466-62045-2322https://doaj.org/article/abc3ebe8a04146e6baa9b970739b961a2021-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-96466-6https://doaj.org/toc/2045-2322Abstract It is important to understand the amino acid residues that govern the properties of the binding between antibodies and ligands. We studied the binding of two anti-norfloxacins, anti-nor 132 and anti-nor 155, and the fluoroquinolones norfloxacin, enrofloxacin, ciprofloxacin, and ofloxacin. Binding cross-reactivities tested by an indirect competitive enzyme-linked immunosorbent assay indicated that anti-nor 132 (22–100%) had a broader range of cross-reactivity than anti-nor 155 (62–100%). These cross-reactivities correlated with variations in the numbers of interacting amino acid residues and their positions. Molecular docking was employed to investigate the molecular interactions between the fluoroquinolones and the monoclonal antibodies. Homology models of the heavy chain and light chain variable regions of each mAb 3D structure were docked with the fluoroquinolones targeting the crucial part of the complementarity-determining regions. The fluoroquinolone binding site of anti-nor 155 was a region of the HCDR3 and LCDR3 loops in which hydrogen bonds were formed with TYR (H:35), ASN (H:101), LYS (H:106), ASN (L:92), and ASN (L:93). These regions were further away in anti-nor 132 and could not contact the fluoroquinolones. Another binding region consisting of HIS (L:38) and ASP (H:100) was found for norfloxacin, enrofloxacin, and ciprofloxacin, whereas only ASP (H:100) was found for ofloxacin.Patamalai BoonsermSongchan PuthongThanaporn WichaiSajee NoitangPongsak KhunraeSarintip SooksaiKittinan KomolpisNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Patamalai Boonserm Songchan Puthong Thanaporn Wichai Sajee Noitang Pongsak Khunrae Sarintip Sooksai Kittinan Komolpis Investigation of major amino acid residues of anti-norfloxacin monoclonal antibodies responsible for binding with fluoroquinolones
description	Abstract It is important to understand the amino acid residues that govern the properties of the binding between antibodies and ligands. We studied the binding of two anti-norfloxacins, anti-nor 132 and anti-nor 155, and the fluoroquinolones norfloxacin, enrofloxacin, ciprofloxacin, and ofloxacin. Binding cross-reactivities tested by an indirect competitive enzyme-linked immunosorbent assay indicated that anti-nor 132 (22–100%) had a broader range of cross-reactivity than anti-nor 155 (62–100%). These cross-reactivities correlated with variations in the numbers of interacting amino acid residues and their positions. Molecular docking was employed to investigate the molecular interactions between the fluoroquinolones and the monoclonal antibodies. Homology models of the heavy chain and light chain variable regions of each mAb 3D structure were docked with the fluoroquinolones targeting the crucial part of the complementarity-determining regions. The fluoroquinolone binding site of anti-nor 155 was a region of the HCDR3 and LCDR3 loops in which hydrogen bonds were formed with TYR (H:35), ASN (H:101), LYS (H:106), ASN (L:92), and ASN (L:93). These regions were further away in anti-nor 132 and could not contact the fluoroquinolones. Another binding region consisting of HIS (L:38) and ASP (H:100) was found for norfloxacin, enrofloxacin, and ciprofloxacin, whereas only ASP (H:100) was found for ofloxacin.
format	article
author	Patamalai Boonserm Songchan Puthong Thanaporn Wichai Sajee Noitang Pongsak Khunrae Sarintip Sooksai Kittinan Komolpis
author_facet	Patamalai Boonserm Songchan Puthong Thanaporn Wichai Sajee Noitang Pongsak Khunrae Sarintip Sooksai Kittinan Komolpis
author_sort	Patamalai Boonserm
title	Investigation of major amino acid residues of anti-norfloxacin monoclonal antibodies responsible for binding with fluoroquinolones
title_short	Investigation of major amino acid residues of anti-norfloxacin monoclonal antibodies responsible for binding with fluoroquinolones
title_full	Investigation of major amino acid residues of anti-norfloxacin monoclonal antibodies responsible for binding with fluoroquinolones
title_fullStr	Investigation of major amino acid residues of anti-norfloxacin monoclonal antibodies responsible for binding with fluoroquinolones
title_full_unstemmed	Investigation of major amino acid residues of anti-norfloxacin monoclonal antibodies responsible for binding with fluoroquinolones
title_sort	investigation of major amino acid residues of anti-norfloxacin monoclonal antibodies responsible for binding with fluoroquinolones
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/abc3ebe8a04146e6baa9b970739b961a
work_keys_str_mv	AT patamalaiboonserm investigationofmajoraminoacidresiduesofantinorfloxacinmonoclonalantibodiesresponsibleforbindingwithfluoroquinolones AT songchanputhong investigationofmajoraminoacidresiduesofantinorfloxacinmonoclonalantibodiesresponsibleforbindingwithfluoroquinolones AT thanapornwichai investigationofmajoraminoacidresiduesofantinorfloxacinmonoclonalantibodiesresponsibleforbindingwithfluoroquinolones AT sajeenoitang investigationofmajoraminoacidresiduesofantinorfloxacinmonoclonalantibodiesresponsibleforbindingwithfluoroquinolones AT pongsakkhunrae investigationofmajoraminoacidresiduesofantinorfloxacinmonoclonalantibodiesresponsibleforbindingwithfluoroquinolones AT sarintipsooksai investigationofmajoraminoacidresiduesofantinorfloxacinmonoclonalantibodiesresponsibleforbindingwithfluoroquinolones AT kittinankomolpis investigationofmajoraminoacidresiduesofantinorfloxacinmonoclonalantibodiesresponsibleforbindingwithfluoroquinolones
_version_	1718387832498683904

Investigation of major amino acid residues of anti-norfloxacin monoclonal antibodies responsible for binding with fluoroquinolones

Ejemplares similares