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

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Anti-endotoxic and antibacterial effects of a dermal substitute coated with host defense peptides. / Kasetty, Gopinath; Kalle, Martina; Mörgelin, Matthias; Brune, Jan Claas; Schmidtchen, Artur.

In: Biomaterials, Vol. 53, 2015, p. 415-425.

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Kasetty, Gopinath ; Kalle, Martina ; Mörgelin, Matthias ; Brune, Jan Claas ; Schmidtchen, Artur. / Anti-endotoxic and antibacterial effects of a dermal substitute coated with host defense peptides. In: Biomaterials. 2015 ; Vol. 53. pp. 415-425.

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TY - JOUR

T1 - Anti-endotoxic and antibacterial effects of a dermal substitute coated with host defense peptides.

AU - Kasetty, Gopinath

AU - Kalle, Martina

AU - Mörgelin, Matthias

AU - Brune, Jan Claas

AU - Schmidtchen, Artur

PY - 2015

Y1 - 2015

N2 - 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(®)). 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.

AB - 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(®)). 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.

U2 - 10.1016/j.biomaterials.2015.02.111

DO - 10.1016/j.biomaterials.2015.02.111

M3 - Article

VL - 53

SP - 415

EP - 425

JO - Biomaterials

T2 - Biomaterials

JF - Biomaterials

SN - 1878-5905

ER -