The lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences

Clark et al. comprehensively explore the primary structural features underlying the activity of a complete set of antimicrobial peptides (AMPs). They find that the shortest active peptides were 4 or 5 residues in length, with activity being associated with 40% arginine, and multiple adjacent tryptop...

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Autores principales:	Sam Clark, Thomas A. Jowitt, Lynda K. Harris, Christopher G. Knight, Curtis B. Dobson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/07077bdf64fe48439afbfe1eab85d91f
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spelling	oai:doaj.org-article:07077bdf64fe48439afbfe1eab85d91f2021-12-02T16:49:37ZThe lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences10.1038/s42003-021-02137-72399-3642https://doaj.org/article/07077bdf64fe48439afbfe1eab85d91f2021-05-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02137-7https://doaj.org/toc/2399-3642Clark et al. comprehensively explore the primary structural features underlying the activity of a complete set of antimicrobial peptides (AMPs). They find that the shortest active peptides were 4 or 5 residues in length, with activity being associated with 40% arginine, and multiple adjacent tryptophan residues. This study provides insights into the design of effective AMPs.Sam ClarkThomas A. JowittLynda K. HarrisChristopher G. KnightCurtis B. DobsonNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Sam Clark Thomas A. Jowitt Lynda K. Harris Christopher G. Knight Curtis B. Dobson The lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences
description	Clark et al. comprehensively explore the primary structural features underlying the activity of a complete set of antimicrobial peptides (AMPs). They find that the shortest active peptides were 4 or 5 residues in length, with activity being associated with 40% arginine, and multiple adjacent tryptophan residues. This study provides insights into the design of effective AMPs.
format	article
author	Sam Clark Thomas A. Jowitt Lynda K. Harris Christopher G. Knight Curtis B. Dobson
author_facet	Sam Clark Thomas A. Jowitt Lynda K. Harris Christopher G. Knight Curtis B. Dobson
author_sort	Sam Clark
title	The lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences
title_short	The lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences
title_full	The lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences
title_fullStr	The lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences
title_full_unstemmed	The lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences
title_sort	lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/07077bdf64fe48439afbfe1eab85d91f
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The lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences

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