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Altering the Peptide Binding Selectivity of Polymeric Reverse Micelle Assemblies via Metal Ion Loading

[Image: see text] Supramolecular reverse micelle assemblies, formed by amphiphilic copolymers, can selectively encapsulate molecules in their interiors depending on the functional groups present in the polymers. Altering the binding selectivity of these materials typically requires the synthesis of...

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Autores principales: Wang, Meizhe, Zhao, Bo, Gao, Jingjing, He, Huan, Castellanos, Laura J., Thayumanavan, S., Vachet, Richard W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2017
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5730948/
https://www.ncbi.nlm.nih.gov/pubmed/28803471
http://dx.doi.org/10.1021/acs.langmuir.7b02488
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author Wang, Meizhe
Zhao, Bo
Gao, Jingjing
He, Huan
Castellanos, Laura J.
Thayumanavan, S.
Vachet, Richard W.
author_facet Wang, Meizhe
Zhao, Bo
Gao, Jingjing
He, Huan
Castellanos, Laura J.
Thayumanavan, S.
Vachet, Richard W.
author_sort Wang, Meizhe
collection PubMed
description [Image: see text] Supramolecular reverse micelle assemblies, formed by amphiphilic copolymers, can selectively encapsulate molecules in their interiors depending on the functional groups present in the polymers. Altering the binding selectivity of these materials typically requires the synthesis of alternate functional groups. Here, we demonstrate that the addition of Zr(IV) ions to the interiors of reverse micelles having phosphonate functional groups transforms the supramolecular materials from ones that selectively bind positively charged peptides into materials that selectively bind phosphorylated peptides. We also show that the binding selectivity of these reverse micelle assemblies can be further tuned by varying the fractions of phosphonate groups in the copolymer structure. The optimized reverse micelle materials can selectively transfer and bind phosphorylated peptides from aqueous solutions over a wide range of pH conditions and can selectively enrich phosphorylated peptides even in complicated mixtures.
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spelling pubmed-57309482017-12-17 Altering the Peptide Binding Selectivity of Polymeric Reverse Micelle Assemblies via Metal Ion Loading Wang, Meizhe Zhao, Bo Gao, Jingjing He, Huan Castellanos, Laura J. Thayumanavan, S. Vachet, Richard W. Langmuir [Image: see text] Supramolecular reverse micelle assemblies, formed by amphiphilic copolymers, can selectively encapsulate molecules in their interiors depending on the functional groups present in the polymers. Altering the binding selectivity of these materials typically requires the synthesis of alternate functional groups. Here, we demonstrate that the addition of Zr(IV) ions to the interiors of reverse micelles having phosphonate functional groups transforms the supramolecular materials from ones that selectively bind positively charged peptides into materials that selectively bind phosphorylated peptides. We also show that the binding selectivity of these reverse micelle assemblies can be further tuned by varying the fractions of phosphonate groups in the copolymer structure. The optimized reverse micelle materials can selectively transfer and bind phosphorylated peptides from aqueous solutions over a wide range of pH conditions and can selectively enrich phosphorylated peptides even in complicated mixtures. American Chemical Society 2017-08-11 2017-12-12 /pmc/articles/PMC5730948/ /pubmed/28803471 http://dx.doi.org/10.1021/acs.langmuir.7b02488 Text en Copyright © 2017 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Wang, Meizhe
Zhao, Bo
Gao, Jingjing
He, Huan
Castellanos, Laura J.
Thayumanavan, S.
Vachet, Richard W.
Altering the Peptide Binding Selectivity of Polymeric Reverse Micelle Assemblies via Metal Ion Loading
title Altering the Peptide Binding Selectivity of Polymeric Reverse Micelle Assemblies via Metal Ion Loading
title_full Altering the Peptide Binding Selectivity of Polymeric Reverse Micelle Assemblies via Metal Ion Loading
title_fullStr Altering the Peptide Binding Selectivity of Polymeric Reverse Micelle Assemblies via Metal Ion Loading
title_full_unstemmed Altering the Peptide Binding Selectivity of Polymeric Reverse Micelle Assemblies via Metal Ion Loading
title_short Altering the Peptide Binding Selectivity of Polymeric Reverse Micelle Assemblies via Metal Ion Loading
title_sort altering the peptide binding selectivity of polymeric reverse micelle assemblies via metal ion loading
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5730948/
https://www.ncbi.nlm.nih.gov/pubmed/28803471
http://dx.doi.org/10.1021/acs.langmuir.7b02488
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