Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides

Thrombin-derived C-terminal peptides (TCPs) have anti-endotoxic functions in wounds by binding to bacterial lipopolysaccharide (LPS) and Gram-negative bacteria. Here authors use a spectrum of biophysical techniques to determine the conformation of a TCP in complex with LPS and define the interaction...

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Autores principales:	Rathi Saravanan, Daniel A Holdbrook, Jitka Petrlova, Shalini Singh, Nils A Berglund, Yeu Khai Choong, Sven Kjellström, Peter J Bond, Martin Malmsten, Artur Schmidtchen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/637ac0a8256041d7988e22fb5b99d12e
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spelling	oai:doaj.org-article:637ac0a8256041d7988e22fb5b99d12e2021-12-02T14:39:47ZStructural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides10.1038/s41467-018-05242-02041-1723https://doaj.org/article/637ac0a8256041d7988e22fb5b99d12e2018-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05242-0https://doaj.org/toc/2041-1723Thrombin-derived C-terminal peptides (TCPs) have anti-endotoxic functions in wounds by binding to bacterial lipopolysaccharide (LPS) and Gram-negative bacteria. Here authors use a spectrum of biophysical techniques to determine the conformation of a TCP in complex with LPS and define the interaction between TCPs and CD14.Rathi SaravananDaniel A HoldbrookJitka PetrlovaShalini SinghNils A BerglundYeu Khai ChoongSven KjellströmPeter J BondMartin MalmstenArtur SchmidtchenNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Rathi Saravanan Daniel A Holdbrook Jitka Petrlova Shalini Singh Nils A Berglund Yeu Khai Choong Sven Kjellström Peter J Bond Martin Malmsten Artur Schmidtchen Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides
description	Thrombin-derived C-terminal peptides (TCPs) have anti-endotoxic functions in wounds by binding to bacterial lipopolysaccharide (LPS) and Gram-negative bacteria. Here authors use a spectrum of biophysical techniques to determine the conformation of a TCP in complex with LPS and define the interaction between TCPs and CD14.
format	article
author	Rathi Saravanan Daniel A Holdbrook Jitka Petrlova Shalini Singh Nils A Berglund Yeu Khai Choong Sven Kjellström Peter J Bond Martin Malmsten Artur Schmidtchen
author_facet	Rathi Saravanan Daniel A Holdbrook Jitka Petrlova Shalini Singh Nils A Berglund Yeu Khai Choong Sven Kjellström Peter J Bond Martin Malmsten Artur Schmidtchen
author_sort	Rathi Saravanan
title	Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides
title_short	Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides
title_full	Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides
title_fullStr	Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides
title_full_unstemmed	Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides
title_sort	structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived c-terminal peptides
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/637ac0a8256041d7988e22fb5b99d12e
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Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides

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