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The complete excretion/secretion product of Lucilia sericata maggots was screened for therapeutically active propeptides and peptides by performing a classical, gel- based proteomic study.

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Academic year: 2021

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Abstract______________________________________________________________

Abstract:

Maggot therapy is a simple and highly successful treatment used for centuries for the clearing of necrotic and infected wounds. Recently, the application of maggot treatment became increasingly important for the treatment of non-healing wounds, which are infected by multi-drug resistant pathogens, especially methicillin-resistent Staphylococcus aureus . The aim of this thesis was to identify and characterise antibacterial substances produced by maggots of the greenbottle fly Lucilia sericata . To approach this problem we analysed both the secretions of salivary glands as well as the content of the excretion/secretion product of Lucilia sericata maggots. In the peptidome of the salivary glands we identified a peptide fragment generated from the ß-subunit of the protein inhibin. This protein is related to the short protein activin, derived from the ß-subunit of Inhibin, which plays an important role in wound healing.

The complete excretion/secretion product of Lucilia sericata maggots was screened for therapeutically active propeptides and peptides by performing a classical, gel- based proteomic study.

In the small protein fraction we identified a dermaseptin-like protein. This protein showed powerful effects against gram negative and gram positive bacteria.

The peptide fraction of the ES-product expressed a potent anti-bacterial activity

against Staphylococcus aureus in vitro . Biochemical purification by two-dimensional

chromatography over reversed-phase and hydrophilic columns resulted in the

isolation of fraction with activity against Staphylococcus aureus . By mass

spectrometry a single dominant at m/z 1060 Da was identified in active fractions. By

LS-ESI/MS/MS of active fractions a nonapeptide was partially sequenced: S-Y-

A(N,F,V)A-Y-D. A final assignment of biological activity and peptide structure

remains to be achieved by further structural analysis.

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