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Biochim Biophys Acta. 2014 Oct;1838(10):2739-44. doi: 10.1016/j.bbamem.2014.07.005. Epub 2014 Jul 10.

Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) anti-bacterial and anti-endotoxic effects.

Author information

1
Instituto de Química, Facultad de Ciencias Exactas y Naturales, Universidad de Antioquia, AA. 1226, Medellín, Colombia.. Electronic address: wilcova@gmail.com.
2
Instituto de Química, Facultad de Ciencias Exactas y Naturales, Universidad de Antioquia, AA. 1226, Medellín, Colombia.. Electronic address: mmanriqm@exactas.udea.edu.co.
3
Forschungszentrum Borstel, Division of Biophysics, Parkallee 10, 23845 Borstel, Germany. Electronic address: jbehrends@fz-borstel.de.
4
Instituto de Química, Facultad de Ciencias Exactas y Naturales, Universidad de Antioquia, AA. 1226, Medellín, Colombia.. Electronic address: epatino@matematicas.udea.edu.co.
5
Forschungszentrum Borstel, Division of Biophysics, Parkallee 10, 23845 Borstel, Germany. Electronic address: cmarella@fz-borstel.de.
6
Instituto de Química, Facultad de Ciencias Exactas y Naturales, Universidad de Antioquia, AA. 1226, Medellín, Colombia.. Electronic address: directorgiem@gmail.com.
7
Universität Halle-Wiienberg, Institut für Physikalische Chemie, Von-Danckelmann-Platz 4, 06120 Halle/Saale, Germany. Electronic address: Patrick.Garidel@chemie.uni-halle.de.
8
Forschungszentrum Borstel, Division of Biophysics, Parkallee 10, 23845 Borstel, Germany. Electronic address: tgutsmann@fz-borstel.de.
9
Forschungszentrum Borstel, Division of Biophysics, Parkallee 10, 23845 Borstel, Germany. Electronic address: kbrandenburg@fz-borstel.de.
10
Forschungszentrum Borstel, Division of Biophysics, Parkallee 10, 23845 Borstel, Germany. Electronic address: lheinbockel@fz-borstel.de.

Abstract

Antimicrobial peptides (AMPs) are important components of the innate immune system of animals, plants, fungi and bacteria and are recently under discussion as promising alternatives to conventional antibiotics. We have investigated two cecropin-like synthetic peptides, Gm1, which corresponds to the natural overall uncharged Galleria mellonella native peptide and ΔGm1, a modified overall positively charged Gm1 variant. We have analysed these peptides for their potential to inhibit the endotoxin-induced secretion of tumour necrosis factor-α (TNF-α) from human mononuclear cells. Furthermore, in a conventional microbiological assay, the ability of these peptides to inhibit the growth of the rough mutant bacteria Salmonella enterica Minnesota R60 and the polymyxin B-resistant Proteus mirabilis R45 was investigated and atomic force microscopy (AFM) measurements were performed to characterize the morphology of the bacteria treated by the two peptides. We have also studied their cytotoxic properties in a haemolysis assay to clarify potential toxic effects. Our data revealed for both peptides minor anti-inflammatory (anti-endotoxin) activity, but demonstrated antimicrobial activity with differences depending on the endotoxin composition of the respective bacteria. In accordance with the antimicrobial assay, AFM data revealed a stronger morphology change of the R45 bacteria than for the R60. Furthermore, Gm1 had a stronger effect on the bacteria than ΔGm1, leading to a different morphology regarding indentations and coalescing of bacterial structures. The findings verify the biophysical measurements with the peptides on model systems. Both peptides lack any haemolytic activity up to an amount of 100μg/ml, making them suitable as new anti-infective agents.

KEYWORDS:

Antibacterial/antimicrobial peptide; Atomic force microscopy; Galleria mellonella; Lipopolysaccharide; Peptide-lipid interaction

PMID:
25016054
DOI:
10.1016/j.bbamem.2014.07.005
[Indexed for MEDLINE]
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