A minimalistic cyclic ice-binding peptide from phage display

Developing molecules that emulate the properties of naturally occurring ice-binding proteins (IBPs) is a daunting challenge. Here, the authors demonstrate the use of phage display for the identification of short peptide mimics of IBPs, which resulted in the identification of a cyclic ice-binding pep...

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Autores principales:	Corey A. Stevens, Fabienne Bachtiger, Xu-Dong Kong, Luciano A. Abriata, Gabriele C. Sosso, Matthew I. Gibson, Harm-Anton Klok
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/21547cda4f1a4a8ab88ce626361f17f5
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spelling	oai:doaj.org-article:21547cda4f1a4a8ab88ce626361f17f52021-12-02T17:02:20ZA minimalistic cyclic ice-binding peptide from phage display10.1038/s41467-021-22883-w2041-1723https://doaj.org/article/21547cda4f1a4a8ab88ce626361f17f52021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22883-whttps://doaj.org/toc/2041-1723Developing molecules that emulate the properties of naturally occurring ice-binding proteins (IBPs) is a daunting challenge. Here, the authors demonstrate the use of phage display for the identification of short peptide mimics of IBPs, which resulted in the identification of a cyclic ice-binding peptide containing just 14 amino acids.Corey A. StevensFabienne BachtigerXu-Dong KongLuciano A. AbriataGabriele C. SossoMatthew I. GibsonHarm-Anton KlokNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Corey A. Stevens Fabienne Bachtiger Xu-Dong Kong Luciano A. Abriata Gabriele C. Sosso Matthew I. Gibson Harm-Anton Klok A minimalistic cyclic ice-binding peptide from phage display
description	Developing molecules that emulate the properties of naturally occurring ice-binding proteins (IBPs) is a daunting challenge. Here, the authors demonstrate the use of phage display for the identification of short peptide mimics of IBPs, which resulted in the identification of a cyclic ice-binding peptide containing just 14 amino acids.
format	article
author	Corey A. Stevens Fabienne Bachtiger Xu-Dong Kong Luciano A. Abriata Gabriele C. Sosso Matthew I. Gibson Harm-Anton Klok
author_facet	Corey A. Stevens Fabienne Bachtiger Xu-Dong Kong Luciano A. Abriata Gabriele C. Sosso Matthew I. Gibson Harm-Anton Klok
author_sort	Corey A. Stevens
title	A minimalistic cyclic ice-binding peptide from phage display
title_short	A minimalistic cyclic ice-binding peptide from phage display
title_full	A minimalistic cyclic ice-binding peptide from phage display
title_fullStr	A minimalistic cyclic ice-binding peptide from phage display
title_full_unstemmed	A minimalistic cyclic ice-binding peptide from phage display
title_sort	minimalistic cyclic ice-binding peptide from phage display
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/21547cda4f1a4a8ab88ce626361f17f5
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A minimalistic cyclic ice-binding peptide from phage display

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