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

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 correspon...

Full description

Autores:
Correa Vargas, Wilmar Alexander
Manrique Moreno, Marcela María
Patiño González, Edwin Bairon
Peláez Jaramillo, Carlos Alberto
Behrends, Jochen
Marella, Chakravarthy
Gutsmann, Thomas
Brandenburg, Klaus
Heinbockel, Lena
Chakravarthy, Marella
Tipo de recurso:
Article of investigation
Fecha de publicación:
2014
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
eng
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/34486
Acceso en línea:
https://hdl.handle.net/10495/34486
Palabra clave:
Lipopolysaccharides - toxicity
Lipopolisacáridos - toxicidad
Anti-Bacterial Agents
Antibacterianos
Microscopy, Atomic Force
Microscopía de Fuerza Atómica
Antimicrobial Cationic Peptides
Péptidos Catiónicos Antimicrobianos
Cells, Cultured
Células Cultivadas
Endotoxemia
Insect Proteins
Proteínas de Insectos
Leukocytes, Mononuclear
Leucocitos Mononucleares
Moths - chemistry
Mariposas Nocturnas - química
Tumor Necrosis Factor-alpha
Factor de Necrosis Tumoral alfa
Galleria mellonella
Rights
openAccess
License
http://creativecommons.org/licenses/by-nc-nd/2.5/co/
id UDEA2_d3446f91b45e2e17a4a7d9c1e32b561d
oai_identifier_str oai:bibliotecadigital.udea.edu.co:10495/34486
network_acronym_str UDEA2
network_name_str Repositorio UdeA
repository_id_str
dc.title.spa.fl_str_mv Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) Anti-bacterial and anti-endotoxic effects
title Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) Anti-bacterial and anti-endotoxic effects
spellingShingle Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) Anti-bacterial and anti-endotoxic effects
Lipopolysaccharides - toxicity
Lipopolisacáridos - toxicidad
Anti-Bacterial Agents
Antibacterianos
Microscopy, Atomic Force
Microscopía de Fuerza Atómica
Antimicrobial Cationic Peptides
Péptidos Catiónicos Antimicrobianos
Cells, Cultured
Células Cultivadas
Endotoxemia
Insect Proteins
Proteínas de Insectos
Leukocytes, Mononuclear
Leucocitos Mononucleares
Moths - chemistry
Mariposas Nocturnas - química
Tumor Necrosis Factor-alpha
Factor de Necrosis Tumoral alfa
Galleria mellonella
title_short Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) Anti-bacterial and anti-endotoxic effects
title_full Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) Anti-bacterial and anti-endotoxic effects
title_fullStr Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) Anti-bacterial and anti-endotoxic effects
title_full_unstemmed Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) Anti-bacterial and anti-endotoxic effects
title_sort Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) Anti-bacterial and anti-endotoxic effects
dc.creator.fl_str_mv Correa Vargas, Wilmar Alexander
Manrique Moreno, Marcela María
Patiño González, Edwin Bairon
Peláez Jaramillo, Carlos Alberto
Behrends, Jochen
Marella, Chakravarthy
Gutsmann, Thomas
Brandenburg, Klaus
Heinbockel, Lena
Chakravarthy, Marella
dc.contributor.author.none.fl_str_mv Correa Vargas, Wilmar Alexander
Manrique Moreno, Marcela María
Patiño González, Edwin Bairon
Peláez Jaramillo, Carlos Alberto
Behrends, Jochen
Marella, Chakravarthy
Gutsmann, Thomas
Brandenburg, Klaus
Heinbockel, Lena
Chakravarthy, Marella
dc.contributor.researchgroup.spa.fl_str_mv Grupo Interdisciplinario de Estudios Moleculares
dc.subject.decs.none.fl_str_mv Lipopolysaccharides - toxicity
Lipopolisacáridos - toxicidad
Anti-Bacterial Agents
Antibacterianos
Microscopy, Atomic Force
Microscopía de Fuerza Atómica
Antimicrobial Cationic Peptides
Péptidos Catiónicos Antimicrobianos
Cells, Cultured
Células Cultivadas
Endotoxemia
Insect Proteins
Proteínas de Insectos
Leukocytes, Mononuclear
Leucocitos Mononucleares
Moths - chemistry
Mariposas Nocturnas - química
Tumor Necrosis Factor-alpha
Factor de Necrosis Tumoral alfa
topic Lipopolysaccharides - toxicity
Lipopolisacáridos - toxicidad
Anti-Bacterial Agents
Antibacterianos
Microscopy, Atomic Force
Microscopía de Fuerza Atómica
Antimicrobial Cationic Peptides
Péptidos Catiónicos Antimicrobianos
Cells, Cultured
Células Cultivadas
Endotoxemia
Insect Proteins
Proteínas de Insectos
Leukocytes, Mononuclear
Leucocitos Mononucleares
Moths - chemistry
Mariposas Nocturnas - química
Tumor Necrosis Factor-alpha
Factor de Necrosis Tumoral alfa
Galleria mellonella
dc.subject.proposal.spa.fl_str_mv Galleria mellonella
description 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 anti- microbial activity with differences depending on the endotoxin composition of the respective bacteria. In accor- dance 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 100 μg/ml, making them suitable as new anti-infective agents.
publishDate 2014
dc.date.issued.none.fl_str_mv 2014
dc.date.accessioned.none.fl_str_mv 2023-04-06T23:48:12Z
dc.date.available.none.fl_str_mv 2023-04-06T23:48:12Z
dc.type.spa.fl_str_mv Artículo de investigación
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dc.identifier.citation.spa.fl_str_mv Correa W, Manrique-Moreno M, Behrends J, Patiño E, Marella C, Peláez-Jaramillo C, Garidel P, Gutsmann T, Brandenburg K, Heinbockel L. Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) anti-bacterial and anti-endotoxic effects. Biochim Biophys Acta. 2014 Oct;1838(10):2739-44. doi: 10.1016/j.bbamem.2014.07.005.
dc.identifier.issn.none.fl_str_mv 0006-3002
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/10495/34486
dc.identifier.doi.none.fl_str_mv 10.1016/j.bbamem.2014.07.005
dc.identifier.eissn.none.fl_str_mv 1878-2434
identifier_str_mv Correa W, Manrique-Moreno M, Behrends J, Patiño E, Marella C, Peláez-Jaramillo C, Garidel P, Gutsmann T, Brandenburg K, Heinbockel L. Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) anti-bacterial and anti-endotoxic effects. Biochim Biophys Acta. 2014 Oct;1838(10):2739-44. doi: 10.1016/j.bbamem.2014.07.005.
0006-3002
10.1016/j.bbamem.2014.07.005
1878-2434
url https://hdl.handle.net/10495/34486
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.ispartofjournalabbrev.spa.fl_str_mv Biochim. Biophys. Acta.
dc.relation.citationendpage.spa.fl_str_mv 2744
dc.relation.citationissue.spa.fl_str_mv 10
dc.relation.citationstartpage.spa.fl_str_mv 2739
dc.relation.citationvolume.spa.fl_str_mv 1838
dc.relation.ispartofjournal.spa.fl_str_mv Biochimica et Biophysica Acta
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dc.publisher.spa.fl_str_mv Elsevier
dc.publisher.place.spa.fl_str_mv Ámsterdam, Países Bajos
institution Universidad de Antioquia
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spelling Correa Vargas, Wilmar AlexanderManrique Moreno, Marcela MaríaPatiño González, Edwin BaironPeláez Jaramillo, Carlos AlbertoBehrends, JochenMarella, ChakravarthyGutsmann, ThomasBrandenburg, KlausHeinbockel, LenaChakravarthy, MarellaGrupo Interdisciplinario de Estudios Moleculares2023-04-06T23:48:12Z2023-04-06T23:48:12Z2014Correa W, Manrique-Moreno M, Behrends J, Patiño E, Marella C, Peláez-Jaramillo C, Garidel P, Gutsmann T, Brandenburg K, Heinbockel L. Galleria mellonella native and analogue peptides Gm1 and ΔGm1. II) anti-bacterial and anti-endotoxic effects. Biochim Biophys Acta. 2014 Oct;1838(10):2739-44. doi: 10.1016/j.bbamem.2014.07.005.0006-3002https://hdl.handle.net/10495/3448610.1016/j.bbamem.2014.07.0051878-2434ABSTRACT: 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 anti- microbial activity with differences depending on the endotoxin composition of the respective bacteria. In accor- dance 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 100 μg/ml, making them suitable as new anti-infective agents.COL00074626application/pdfengElsevierÁmsterdam, Países Bajoshttp://creativecommons.org/licenses/by-nc-nd/2.5/co/https://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Galleria mellonella native and analogue peptides Gm1 and ΔGm1. 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