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Surfactant-Assisted Assembly of Dipeptide Forming a Broom-like Structure

Understanding the influence of surfactants on the assembly of peptides has a considerable practical motivation. In this paper, we systematically study the anionic surfactant-assisted assembly of diphenylalanine (FF). FF forms broom-like structures in a concentration of sodium cholate (NaC) around th...

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Detalles Bibliográficos
Autores principales: Wei, Yunping, Zhang, Jie, Liu, Xingcen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9369827/
https://www.ncbi.nlm.nih.gov/pubmed/35956826
http://dx.doi.org/10.3390/molecules27154876
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author Wei, Yunping
Zhang, Jie
Liu, Xingcen
author_facet Wei, Yunping
Zhang, Jie
Liu, Xingcen
author_sort Wei, Yunping
collection PubMed
description Understanding the influence of surfactants on the assembly of peptides has a considerable practical motivation. In this paper, we systematically study the anionic surfactant-assisted assembly of diphenylalanine (FF). FF forms broom-like structures in a concentration of sodium cholate (NaC) around the CMC, and assembles into linear and unidirectional rods in the presence of low and high surfactant concentrations. FF’s improved hydrogen bonding and controlled assembly rates are appropriate for other anionic surfactants. At this stage, the use of FF as the simplest protein consequence can be helpful in the investigation of further protein–surfactant interactions.
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spelling pubmed-93698272022-08-12 Surfactant-Assisted Assembly of Dipeptide Forming a Broom-like Structure Wei, Yunping Zhang, Jie Liu, Xingcen Molecules Communication Understanding the influence of surfactants on the assembly of peptides has a considerable practical motivation. In this paper, we systematically study the anionic surfactant-assisted assembly of diphenylalanine (FF). FF forms broom-like structures in a concentration of sodium cholate (NaC) around the CMC, and assembles into linear and unidirectional rods in the presence of low and high surfactant concentrations. FF’s improved hydrogen bonding and controlled assembly rates are appropriate for other anionic surfactants. At this stage, the use of FF as the simplest protein consequence can be helpful in the investigation of further protein–surfactant interactions. MDPI 2022-07-29 /pmc/articles/PMC9369827/ /pubmed/35956826 http://dx.doi.org/10.3390/molecules27154876 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Communication
Wei, Yunping
Zhang, Jie
Liu, Xingcen
Surfactant-Assisted Assembly of Dipeptide Forming a Broom-like Structure
title Surfactant-Assisted Assembly of Dipeptide Forming a Broom-like Structure
title_full Surfactant-Assisted Assembly of Dipeptide Forming a Broom-like Structure
title_fullStr Surfactant-Assisted Assembly of Dipeptide Forming a Broom-like Structure
title_full_unstemmed Surfactant-Assisted Assembly of Dipeptide Forming a Broom-like Structure
title_short Surfactant-Assisted Assembly of Dipeptide Forming a Broom-like Structure
title_sort surfactant-assisted assembly of dipeptide forming a broom-like structure
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9369827/
https://www.ncbi.nlm.nih.gov/pubmed/35956826
http://dx.doi.org/10.3390/molecules27154876
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