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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Main Authors: Rathi Saravanan, Daniel A Holdbrook, Jitka Petrlova, Shalini Singh, Nils A Berglund, Yeu Khai Choong, Sven Kjellström, Peter J Bond, Martin Malmsten, Artur Schmidtchen
Format: Article
Language:English
Published: Nature Portfolio 2018-07-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-05242-0
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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
collection DOAJ
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.
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spelling doaj.art-637ac0a8256041d7988e22fb5b99d12e2022-12-21T23:00:44ZengNature PortfolioNature Communications2041-17232018-07-019111410.1038/s41467-018-05242-0Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptidesRathi Saravanan0Daniel A Holdbrook1Jitka Petrlova2Shalini Singh3Nils A Berglund4Yeu Khai Choong5Sven Kjellström6Peter J Bond7Martin Malmsten8Artur Schmidtchen9Lee Kong Chian School of Medicine, Nanyang Technological UniversityBioinformatics Institute (A*STAR)Division of Dermatology and Venereology, Department of Clinical Sciences, Lund UniversityDepartment of Pharmacy, Uppsala UniversityBioinformatics Institute (A*STAR)Lee Kong Chian School of Medicine, Nanyang Technological UniversityCentre of Excellence in Biological and Medical Mass Spectrometry (CEBMMS), Biomedical Centre D13, Lund UniversityBioinformatics Institute (A*STAR)Department of Pharmacy, Uppsala UniversityLee Kong Chian School of Medicine, Nanyang Technological UniversityThrombin-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.https://doi.org/10.1038/s41467-018-05242-0
spellingShingle 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
Nature Communications
title 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_short 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
url https://doi.org/10.1038/s41467-018-05242-0
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