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A minimal length rigid helical peptide motif allows rational design of modular surfactants
Extensive work has been invested in the design of bio-inspired peptide emulsifiers. Yet, none of the formulated surfactants were based on the utilization of the robust conformation and self-assembly tendencies presented by the hydrophobins, which exhibited highest surface activity among all known pr...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5241864/ https://www.ncbi.nlm.nih.gov/pubmed/28084315 http://dx.doi.org/10.1038/ncomms14018 |
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author | Mondal, Sudipta Varenik, Maxim Bloch, Daniel Nir Atsmon-Raz, Yoav Jacoby, Guy Adler-Abramovich, Lihi Shimon, Linda J.W. Beck, Roy Miller, Yifat Regev, Oren Gazit, Ehud |
author_facet | Mondal, Sudipta Varenik, Maxim Bloch, Daniel Nir Atsmon-Raz, Yoav Jacoby, Guy Adler-Abramovich, Lihi Shimon, Linda J.W. Beck, Roy Miller, Yifat Regev, Oren Gazit, Ehud |
author_sort | Mondal, Sudipta |
collection | PubMed |
description | Extensive work has been invested in the design of bio-inspired peptide emulsifiers. Yet, none of the formulated surfactants were based on the utilization of the robust conformation and self-assembly tendencies presented by the hydrophobins, which exhibited highest surface activity among all known proteins. Here we show that a minimalist design scheme could be employed to fabricate rigid helical peptides to mimic the rigid conformation and the helical amphipathic organization. These designer building blocks, containing natural non-coded α-aminoisobutyric acid (Aib), form superhelical assemblies as confirmed by crystallography and microscopy. The peptide sequence is amenable to structural modularity and provides the highest stable emulsions reported so far for peptide and protein emulsifiers. Moreover, we establish the ability of short peptides to perform the dual functions of emulsifiers and thickeners, a feature that typically requires synergistic effects of surfactants and polysaccharides. This work provides a different paradigm for the molecular engineering of bioemulsifiers. |
format | Online Article Text |
id | pubmed-5241864 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-52418642017-02-02 A minimal length rigid helical peptide motif allows rational design of modular surfactants Mondal, Sudipta Varenik, Maxim Bloch, Daniel Nir Atsmon-Raz, Yoav Jacoby, Guy Adler-Abramovich, Lihi Shimon, Linda J.W. Beck, Roy Miller, Yifat Regev, Oren Gazit, Ehud Nat Commun Article Extensive work has been invested in the design of bio-inspired peptide emulsifiers. Yet, none of the formulated surfactants were based on the utilization of the robust conformation and self-assembly tendencies presented by the hydrophobins, which exhibited highest surface activity among all known proteins. Here we show that a minimalist design scheme could be employed to fabricate rigid helical peptides to mimic the rigid conformation and the helical amphipathic organization. These designer building blocks, containing natural non-coded α-aminoisobutyric acid (Aib), form superhelical assemblies as confirmed by crystallography and microscopy. The peptide sequence is amenable to structural modularity and provides the highest stable emulsions reported so far for peptide and protein emulsifiers. Moreover, we establish the ability of short peptides to perform the dual functions of emulsifiers and thickeners, a feature that typically requires synergistic effects of surfactants and polysaccharides. This work provides a different paradigm for the molecular engineering of bioemulsifiers. Nature Publishing Group 2017-01-13 /pmc/articles/PMC5241864/ /pubmed/28084315 http://dx.doi.org/10.1038/ncomms14018 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 Mondal, Sudipta Varenik, Maxim Bloch, Daniel Nir Atsmon-Raz, Yoav Jacoby, Guy Adler-Abramovich, Lihi Shimon, Linda J.W. Beck, Roy Miller, Yifat Regev, Oren Gazit, Ehud A minimal length rigid helical peptide motif allows rational design of modular surfactants |
title | A minimal length rigid helical peptide motif allows rational design of modular surfactants |
title_full | A minimal length rigid helical peptide motif allows rational design of modular surfactants |
title_fullStr | A minimal length rigid helical peptide motif allows rational design of modular surfactants |
title_full_unstemmed | A minimal length rigid helical peptide motif allows rational design of modular surfactants |
title_short | A minimal length rigid helical peptide motif allows rational design of modular surfactants |
title_sort | minimal length rigid helical peptide motif allows rational design of modular surfactants |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5241864/ https://www.ncbi.nlm.nih.gov/pubmed/28084315 http://dx.doi.org/10.1038/ncomms14018 |
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