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Major latex-like proteins show pH dependency in their binding to hydrophobic organic pollutants

The Cucurbitaceae family accumulates hydrophobic organic pollutants in its aerial parts at high concentrations. Major latex-like proteins (MLPs) were identified in zucchini (Cucurbita pepo) as a transporting factor for hydrophobic organic pollutants. MLPs bind to hydrophobic organic pollutants in th...

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Detalles Bibliográficos
Autores principales: Fujita, Kentaro, Sonoda, Chihiro, Chujo, Maho, Inui, Hideyuki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Pesticide Science Society of Japan 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10513956/
https://www.ncbi.nlm.nih.gov/pubmed/37745171
http://dx.doi.org/10.1584/jpestics.D23-014
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author Fujita, Kentaro
Sonoda, Chihiro
Chujo, Maho
Inui, Hideyuki
author_facet Fujita, Kentaro
Sonoda, Chihiro
Chujo, Maho
Inui, Hideyuki
author_sort Fujita, Kentaro
collection PubMed
description The Cucurbitaceae family accumulates hydrophobic organic pollutants in its aerial parts at high concentrations. Major latex-like proteins (MLPs) were identified in zucchini (Cucurbita pepo) as a transporting factor for hydrophobic organic pollutants. MLPs bind to hydrophobic organic pollutants in the roots, are secreted to xylem vessels as complexes, and are transported to the aerial parts. However, the suitable conditions for binding MLPs to hydrophobic organic pollutants remain elusive. In the present study, we show that MLPs bind to the hydrophobic organic pollutant pyrene with higher affinity under acidic conditions. Our results demonstrated that pH regulates the binding of MLPs to hydrophobic organic pollutants.
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spelling pubmed-105139562023-09-23 Major latex-like proteins show pH dependency in their binding to hydrophobic organic pollutants Fujita, Kentaro Sonoda, Chihiro Chujo, Maho Inui, Hideyuki J Pestic Sci Regular Article The Cucurbitaceae family accumulates hydrophobic organic pollutants in its aerial parts at high concentrations. Major latex-like proteins (MLPs) were identified in zucchini (Cucurbita pepo) as a transporting factor for hydrophobic organic pollutants. MLPs bind to hydrophobic organic pollutants in the roots, are secreted to xylem vessels as complexes, and are transported to the aerial parts. However, the suitable conditions for binding MLPs to hydrophobic organic pollutants remain elusive. In the present study, we show that MLPs bind to the hydrophobic organic pollutant pyrene with higher affinity under acidic conditions. Our results demonstrated that pH regulates the binding of MLPs to hydrophobic organic pollutants. Pesticide Science Society of Japan 2023-08-20 /pmc/articles/PMC10513956/ /pubmed/37745171 http://dx.doi.org/10.1584/jpestics.D23-014 Text en © 2023 Pesticide Science Society of Japan https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) License.
spellingShingle Regular Article
Fujita, Kentaro
Sonoda, Chihiro
Chujo, Maho
Inui, Hideyuki
Major latex-like proteins show pH dependency in their binding to hydrophobic organic pollutants
title Major latex-like proteins show pH dependency in their binding to hydrophobic organic pollutants
title_full Major latex-like proteins show pH dependency in their binding to hydrophobic organic pollutants
title_fullStr Major latex-like proteins show pH dependency in their binding to hydrophobic organic pollutants
title_full_unstemmed Major latex-like proteins show pH dependency in their binding to hydrophobic organic pollutants
title_short Major latex-like proteins show pH dependency in their binding to hydrophobic organic pollutants
title_sort major latex-like proteins show ph dependency in their binding to hydrophobic organic pollutants
topic Regular Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10513956/
https://www.ncbi.nlm.nih.gov/pubmed/37745171
http://dx.doi.org/10.1584/jpestics.D23-014
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