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A Peptide Amphiphile Organogelator of Polar Organic Solvents

A peptide amphiphile is reported, that gelates a range of polar organic solvents including acetonitrile/water, N,N-dimethylformamide and acetone, in a process dictated by β-sheet interactions and facilitated by the presence of an alkyl chain. Similarities with previously reported peptide amphiphile...

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Detalles Bibliográficos
Autores principales: Rouse, Charlotte K., Martin, Adam D., Easton, Christopher J., Thordarson, Pall
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5334642/
https://www.ncbi.nlm.nih.gov/pubmed/28255169
http://dx.doi.org/10.1038/srep43668
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author Rouse, Charlotte K.
Martin, Adam D.
Easton, Christopher J.
Thordarson, Pall
author_facet Rouse, Charlotte K.
Martin, Adam D.
Easton, Christopher J.
Thordarson, Pall
author_sort Rouse, Charlotte K.
collection PubMed
description A peptide amphiphile is reported, that gelates a range of polar organic solvents including acetonitrile/water, N,N-dimethylformamide and acetone, in a process dictated by β-sheet interactions and facilitated by the presence of an alkyl chain. Similarities with previously reported peptide amphiphile hydrogelators indicate analogous underlying mechanisms of gelation and structure-property relationships, suggesting that peptide amphiphile organogel design may be predictably based on hydrogel precedents.
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spelling pubmed-53346422017-03-06 A Peptide Amphiphile Organogelator of Polar Organic Solvents Rouse, Charlotte K. Martin, Adam D. Easton, Christopher J. Thordarson, Pall Sci Rep Article A peptide amphiphile is reported, that gelates a range of polar organic solvents including acetonitrile/water, N,N-dimethylformamide and acetone, in a process dictated by β-sheet interactions and facilitated by the presence of an alkyl chain. Similarities with previously reported peptide amphiphile hydrogelators indicate analogous underlying mechanisms of gelation and structure-property relationships, suggesting that peptide amphiphile organogel design may be predictably based on hydrogel precedents. Nature Publishing Group 2017-03-03 /pmc/articles/PMC5334642/ /pubmed/28255169 http://dx.doi.org/10.1038/srep43668 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Rouse, Charlotte K.
Martin, Adam D.
Easton, Christopher J.
Thordarson, Pall
A Peptide Amphiphile Organogelator of Polar Organic Solvents
title A Peptide Amphiphile Organogelator of Polar Organic Solvents
title_full A Peptide Amphiphile Organogelator of Polar Organic Solvents
title_fullStr A Peptide Amphiphile Organogelator of Polar Organic Solvents
title_full_unstemmed A Peptide Amphiphile Organogelator of Polar Organic Solvents
title_short A Peptide Amphiphile Organogelator of Polar Organic Solvents
title_sort peptide amphiphile organogelator of polar organic solvents
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5334642/
https://www.ncbi.nlm.nih.gov/pubmed/28255169
http://dx.doi.org/10.1038/srep43668
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