Peptidomic analysis of endogenous and bacterial protease activity in human plasma and wound fluids

Jun Cai, Maike W. Nielsen, Konstantinos Kalogeropoulos, Ulrich auf dem Keller, Mariena J. A. van der Plas*

*Corresponding author for this work

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Abstract

Endogenous and bacterial proteases play important roles in wound healing and infection. Analysis of alterations in the low-molecular-weight peptidome by individual enzymes could therefore provide insight into proteolytic events occurring in wounds and may aid in the discovery of biomarkers. Using liquid chromatography with tandem mass spectrometry, we characterized the peptidome of plasma and acute wound fluids digested ex vivo with human (neutrophil elastase and cathepsin G) and bacterial proteases (Pseudomonas aeruginosa LasB and Staphyloccocus aureus V8). We identified over 100 protein targets for each enzyme and characterized enzyme specific peptides and cleavage patterns. Moreover, we found unique peptide regions in V8 digested samples that were also present in dressing extracts from S. aureus infected wounds. Finally, the work indicates that peptidomic analysis of qualitative differences of proteolytic activity of individual enzymes may aid in the discovery of potential diagnostic biomarkers for wound healing status.
Original languageEnglish
Article number109005
JournaliScience
Volume27
Issue number2
Number of pages19
ISSN2589-0042
DOIs
Publication statusPublished - 2024

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