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Discovery of Surfactant-Like Peptides from a Phage-Displayed Peptide Library

Peptides with specific affinities for various materials have been identified in the past three decades and utilized in materials science and engineering. A peptide’s capability to specifically interact with materials is not naturally derived but screened from a biologically constructed peptide libra...

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Detalles Bibliográficos
Autores principales: Sawada, Toshiki, Oyama, Rina, Tanaka, Michihiro, Serizawa, Takeshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7765448/
https://www.ncbi.nlm.nih.gov/pubmed/33333956
http://dx.doi.org/10.3390/v12121442
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author Sawada, Toshiki
Oyama, Rina
Tanaka, Michihiro
Serizawa, Takeshi
author_facet Sawada, Toshiki
Oyama, Rina
Tanaka, Michihiro
Serizawa, Takeshi
author_sort Sawada, Toshiki
collection PubMed
description Peptides with specific affinities for various materials have been identified in the past three decades and utilized in materials science and engineering. A peptide’s capability to specifically interact with materials is not naturally derived but screened from a biologically constructed peptide library displayed on phages or cells. To date, due to limitations in the screening procedure, the function of screened peptides has been primarily limited to the affinity for target materials. Herein, we demonstrated the screening of surfactant-like peptides from a phage-displayed peptide library. A screened phage clone displaying a peptide showed high activity for accumulating at emulsion surfaces with certain assembled structures, resulting in stable emulsions. The surface tension for the solution of the chemically synthesized peptide decreased with increasing peptide concentration, demonstrating certain surface activity, which corresponded to the ability to decrease the surface tension of liquids (e.g., water), owing to the accumulation of molecules at the air–liquid or liquid–liquid interface. Peptides with a randomized sequence did not lower the surface tension, indicating the essential role of amino acid sequences in surface activity. Our strategy for identifying novel functional peptides from a phage-displayed peptide library can be used to expand the applicability of peptidyl materials and biosurfactants.
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spelling pubmed-77654482020-12-27 Discovery of Surfactant-Like Peptides from a Phage-Displayed Peptide Library Sawada, Toshiki Oyama, Rina Tanaka, Michihiro Serizawa, Takeshi Viruses Article Peptides with specific affinities for various materials have been identified in the past three decades and utilized in materials science and engineering. A peptide’s capability to specifically interact with materials is not naturally derived but screened from a biologically constructed peptide library displayed on phages or cells. To date, due to limitations in the screening procedure, the function of screened peptides has been primarily limited to the affinity for target materials. Herein, we demonstrated the screening of surfactant-like peptides from a phage-displayed peptide library. A screened phage clone displaying a peptide showed high activity for accumulating at emulsion surfaces with certain assembled structures, resulting in stable emulsions. The surface tension for the solution of the chemically synthesized peptide decreased with increasing peptide concentration, demonstrating certain surface activity, which corresponded to the ability to decrease the surface tension of liquids (e.g., water), owing to the accumulation of molecules at the air–liquid or liquid–liquid interface. Peptides with a randomized sequence did not lower the surface tension, indicating the essential role of amino acid sequences in surface activity. Our strategy for identifying novel functional peptides from a phage-displayed peptide library can be used to expand the applicability of peptidyl materials and biosurfactants. MDPI 2020-12-15 /pmc/articles/PMC7765448/ /pubmed/33333956 http://dx.doi.org/10.3390/v12121442 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Sawada, Toshiki
Oyama, Rina
Tanaka, Michihiro
Serizawa, Takeshi
Discovery of Surfactant-Like Peptides from a Phage-Displayed Peptide Library
title Discovery of Surfactant-Like Peptides from a Phage-Displayed Peptide Library
title_full Discovery of Surfactant-Like Peptides from a Phage-Displayed Peptide Library
title_fullStr Discovery of Surfactant-Like Peptides from a Phage-Displayed Peptide Library
title_full_unstemmed Discovery of Surfactant-Like Peptides from a Phage-Displayed Peptide Library
title_short Discovery of Surfactant-Like Peptides from a Phage-Displayed Peptide Library
title_sort discovery of surfactant-like peptides from a phage-displayed peptide library
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7765448/
https://www.ncbi.nlm.nih.gov/pubmed/33333956
http://dx.doi.org/10.3390/v12121442
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