Anti-endotoxic and antibacterial effects of a dermal substitute coated with host defense peptides.

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title = "Anti-endotoxic and antibacterial effects of a dermal substitute coated with host defense peptides.",
abstract = "Biomaterials used during surgery and wound treatment are of increasing importance in modern medical care. In the present study we set out to evaluate the addition of thrombin-derived host defense peptides to human acellular dermis (hAD, i.e. epiflex({\circledR})). Antimicrobial activity of the functionalized hAD was demonstrated using radial diffusion and viable count assays against Gram-negative Escherichia coli, Pseudomonas aeruginosa and Gram-positive Staphylococcus aureus bacteria. Electron microscopy analyses showed that peptide-mediated bacterial killing led to reduced hAD degradation. Furthermore, peptide-functionalized hAD displayed endotoxin-binding activity in vitro, as evidenced by inhibition of NF-κB activation in human monocytic cells (THP-1 cells) and a reduction of pro-inflammatory cytokine production in whole blood in response to lipopolysaccharide stimulation. The dermal substitute retained its anti-endotoxic activity after washing, compatible with results showing that the hAD bound a significant amount of peptide. Furthermore, bacteria-induced contact activation was inhibited by peptide addition to the hAD. E. coli infected hAD, alone, or after treatment with the antiseptic substance polyhexamethylenebiguanide (PHMB), yielded NF-κB activation in THP-1 cells. The activation was abrogated by peptide addition. Thus, thrombin-derived HDPs should be of interest in the further development of new biomaterials with combined antimicrobial and anti-endotoxic functions for use in surgery and wound treatment.",
author = "Gopinath Kasetty and Martina Kalle and Matthias M{\"o}rgelin and Brune, {Jan Claas} and Artur Schmidtchen",
year = "2015",
doi = "10.1016/j.biomaterials.2015.02.111",
language = "English",
volume = "53",
pages = "415--425",
journal = "Biomaterials",
issn = "1878-5905",
publisher = "Elsevier",