<HashMap><database>biostudies-literature</database><scores/><additional><submitter>van der Plas MJ</submitter><funding>Swedish Government Funds for Clinical Research</funding><funding>Stiftelsen Lars Hiertas Minne</funding><funding>Knut and Alice Wallenberg Foundation</funding><funding>LEO Foundation</funding><funding>Hudfonden</funding><funding>Swedish Research Council</funding><funding>OE och Edla Johanssons Vetenskapliga Stiftelse</funding><funding>Alfred Österlunds Stiftelse</funding><funding>Swedish Strategic Research Foundation</funding><funding>Åke Wiberg Stiftelse</funding><funding>Royal Physiographic Society in Lund</funding><funding>VINNOVA</funding><funding>LEO Fondet</funding><pagination>e66876</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8260221</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>10</volume><pubmed_abstract>The normal wound healing process is characterised by proteolytic events, whereas infection results in dysfunctional activations by endogenous and bacterial proteases. Peptides, downstream reporters of these proteolytic actions, could therefore serve as a promising tool for diagnosis of wounds. Using mass-spectrometry analyses, we here for the first time characterise the peptidome of human wound fluids. Sterile post-surgical wound fluids were found to contain a high degree of peptides in comparison to human plasma. Analyses of the peptidome from uninfected healing wounds and &lt;i>Staphylococcus aureus&lt;/i> -infected wounds identify unique peptide patterns of various proteins, including coagulation and complement factors, proteases, and antiproteinases. Together, the work defines a workflow for</pubmed_abstract><journal>eLife</journal><pubmed_title>Method development and characterisation of the low-molecular-weight peptidome of human wound fluids.</pubmed_title><pmcid>PMC8260221</pmcid><funding_grant_id>LF18020</funding_grant_id><funding_grant_id>2017-02341</funding_grant_id><funding_grant_id>2011.0037</funding_grant_id><funding_grant_id>2020-02016</funding_grant_id><pubmed_authors>Saleh K</pubmed_authors><pubmed_authors>Kjellstrom S</pubmed_authors><pubmed_authors>van der Plas MJ</pubmed_authors><pubmed_authors>Cai J</pubmed_authors><pubmed_authors>Petrlova J</pubmed_authors><pubmed_authors>Schmidtchen A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Method development and characterisation of the low-molecular-weight peptidome of human wound fluids.</name><description>The normal wound healing process is characterised by proteolytic events, whereas infection results in dysfunctional activations by endogenous and bacterial proteases. Peptides, downstream reporters of these proteolytic actions, could therefore serve as a promising tool for diagnosis of wounds. Using mass-spectrometry analyses, we here for the first time characterise the peptidome of human wound fluids. Sterile post-surgical wound fluids were found to contain a high degree of peptides in comparison to human plasma. Analyses of the peptidome from uninfected healing wounds and &lt;i>Staphylococcus aureus&lt;/i> -infected wounds identify unique peptide patterns of various proteins, including coagulation and complement factors, proteases, and antiproteinases. Together, the work defines a workflow for</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Jul</publication><modification>2026-05-09T07:51:15.597Z</modification><creation>2022-02-10T18:36:38.258Z</creation></dates><accession>S-EPMC8260221</accession><cross_references><pubmed>34227939</pubmed><doi>10.7554/eLife.66876</doi></cross_references></HashMap>