Method development and characterisation of the low-molecular-weight peptidome of human wound fluids
(2021) In eLife 10.- 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 Staphylococcus aureus-infected wounds identify unique peptide patterns of various proteins, including coagulation and complement factors, proteases, and... (More)
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 Staphylococcus aureus-infected wounds identify unique peptide patterns of various proteins, including coagulation and complement factors, proteases, and antiproteinases. Together, the work defines a workflow for analysis of peptides derived from wound fluids and demonstrates a proof-of-concept that such fluids can be used for analysis of qualitative differences of peptide patterns from larger patient cohorts, providing potential biomarkers for wound healing and infection.
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- author
- van der Plas, Mariena J.A. LU ; Cai, Jun ; Petrlova, Jitka LU ; Saleh, Karim LU ; Kjellström, Sven LU and Schmidtchen, Artur LU
- organization
- publishing date
- 2021
- type
- Contribution to journal
- publication status
- published
- subject
- in
- eLife
- volume
- 10
- article number
- e66876
- publisher
- eLife Sciences Publications
- external identifiers
-
- scopus:85110990648
- pmid:34227939
- ISSN
- 2050-084X
- DOI
- 10.7554/eLife.66876
- language
- English
- LU publication?
- yes
- id
- c27700f5-ca91-4abb-b5a7-dcc63d25edae
- date added to LUP
- 2021-09-14 16:20:08
- date last changed
- 2024-05-04 12:21:15
@article{c27700f5-ca91-4abb-b5a7-dcc63d25edae,
abstract = {{<p>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 Staphylococcus aureus-infected wounds identify unique peptide patterns of various proteins, including coagulation and complement factors, proteases, and antiproteinases. Together, the work defines a workflow for analysis of peptides derived from wound fluids and demonstrates a proof-of-concept that such fluids can be used for analysis of qualitative differences of peptide patterns from larger patient cohorts, providing potential biomarkers for wound healing and infection.</p>}},
author = {{van der Plas, Mariena J.A. and Cai, Jun and Petrlova, Jitka and Saleh, Karim and Kjellström, Sven and Schmidtchen, Artur}},
issn = {{2050-084X}},
language = {{eng}},
publisher = {{eLife Sciences Publications}},
series = {{eLife}},
title = {{Method development and characterisation of the low-molecular-weight peptidome of human wound fluids}},
url = {{http://dx.doi.org/10.7554/eLife.66876}},
doi = {{10.7554/eLife.66876}},
volume = {{10}},
year = {{2021}},
}