Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models
ABSTRACT: Staphylococcus aureus is one of the most pathogenic bacteria; infections with it are associated with significant morbidity and mortality in health care facilities. Antimicrobial peptides are a promising next generation antibiotic with great potential against bacterial infections. In this s...
- Autores:
-
Manrique Moreno, Marcela María
Fandino Devia, Liliana Estefanía
Patino González, Edwin Bairon
Suwalsky, Mario
Jemioła Rzeminska, Małgorzata
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2021
- Institución:
- Universidad de Antioquia
- Repositorio:
- Repositorio UdeA
- Idioma:
- eng
- OAI Identifier:
- oai:bibliotecadigital.udea.edu.co:10495/35232
- Acceso en línea:
- https://hdl.handle.net/10495/35232
- Palabra clave:
- Staphylococcus aureus
Modelos Moleculares
Models, Molecular
Membrana celular
Cell Membrane
Péptidos catiónicos antimicrobianos
Antimicrobial Cationic Peptides
Bicapas lipídicas
Lipid Bilayers
- Rights
- openAccess
- License
- http://creativecommons.org/licenses/by-nc-nd/2.5/co/
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Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models |
| title |
Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models |
| spellingShingle |
Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models Staphylococcus aureus Modelos Moleculares Models, Molecular Membrana celular Cell Membrane Péptidos catiónicos antimicrobianos Antimicrobial Cationic Peptides Bicapas lipídicas Lipid Bilayers |
| title_short |
Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models |
| title_full |
Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models |
| title_fullStr |
Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models |
| title_full_unstemmed |
Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models |
| title_sort |
Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models |
| dc.creator.fl_str_mv |
Manrique Moreno, Marcela María Fandino Devia, Liliana Estefanía Patino González, Edwin Bairon Suwalsky, Mario Jemioła Rzeminska, Małgorzata |
| dc.contributor.author.none.fl_str_mv |
Manrique Moreno, Marcela María Fandino Devia, Liliana Estefanía Patino González, Edwin Bairon Suwalsky, Mario Jemioła Rzeminska, Małgorzata |
| dc.contributor.researchgroup.spa.fl_str_mv |
Grupo de Bioquímica Estructural de Macromoléculas |
| dc.subject.decs.none.fl_str_mv |
Staphylococcus aureus Modelos Moleculares Models, Molecular Membrana celular Cell Membrane Péptidos catiónicos antimicrobianos Antimicrobial Cationic Peptides Bicapas lipídicas Lipid Bilayers |
| topic |
Staphylococcus aureus Modelos Moleculares Models, Molecular Membrana celular Cell Membrane Péptidos catiónicos antimicrobianos Antimicrobial Cationic Peptides Bicapas lipídicas Lipid Bilayers |
| description |
ABSTRACT: Staphylococcus aureus is one of the most pathogenic bacteria; infections with it are associated with significant morbidity and mortality in health care facilities. Antimicrobial peptides are a promising next generation antibiotic with great potential against bacterial infections. In this study, evidence is presented of the biological and biophysical properties of the novel synthetic peptide ΔM3. Its antimicrobial activity against the ATCC 25923 and methicillin-resistant S. aureus strains was evaluated. The results showed that ΔM3 has activity in the same μM range as vancomycin. Biophysical studies were performed with palmitoyloleoylphosphatidylglycerol and cardiolipin liposomes loaded with calcein and used to follow the lytic activity of the peptide by fluorescence spectroscopy. On the other hand, ΔM3 was induced to interact with molecular models of the erythrocyte membrane buil-up of dimiristoylphosphatidylcholine and dimyristoylphosphatidylethanolamine, representative lipids of the outer and inner monolayers of the human erythrocyte membrane, respectively. The capacity of ΔM3 to interact with the bacteria and erythrocyte model membranes was also evaluated by X-ray diffraction and differential scanning calorimetry. The morphological changes induced by the peptide to human erythrocytes were observed by scanning electron microscopy. Results with these techniques indicated that ΔM3 interacted with the inner monolayer of the erythrocyte membrane, which is rich in anionic lipids. Additionally, the cytotoxic effects of ΔM3 on red blood cells were evaluated by monitoring the hemoglobin release from erythrocytes. The results obtained from these different approaches showed ΔM3 to be a non-cytotoxic peptide with antibacterial activity |
| publishDate |
2021 |
| dc.date.issued.none.fl_str_mv |
2021 |
| dc.date.accessioned.none.fl_str_mv |
2023-06-01T15:45:08Z |
| dc.date.available.none.fl_str_mv |
2023-06-01T15:45:08Z |
| dc.type.spa.fl_str_mv |
Artículo de investigación |
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info:eu-repo/semantics/article |
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Manrique-Moreno M, Suwalsky M, Patiño-González E, Fandiño-Devia E, Jemioła-Rzemińska M, Strzałka K. Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models. Biochim Biophys Acta Biomembr. 2021 Feb 1;1863(2):183498. doi: 10.1016/j.bbamem.2020.183498. |
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0005-2736 |
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https://hdl.handle.net/10495/35232 |
| dc.identifier.doi.none.fl_str_mv |
10.1016/j.bbamem.2020.183498 |
| dc.identifier.eissn.none.fl_str_mv |
1879-2642 |
| identifier_str_mv |
Manrique-Moreno M, Suwalsky M, Patiño-González E, Fandiño-Devia E, Jemioła-Rzemińska M, Strzałka K. Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models. Biochim Biophys Acta Biomembr. 2021 Feb 1;1863(2):183498. doi: 10.1016/j.bbamem.2020.183498. 0005-2736 10.1016/j.bbamem.2020.183498 1879-2642 |
| url |
https://hdl.handle.net/10495/35232 |
| dc.language.iso.spa.fl_str_mv |
eng |
| language |
eng |
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Biochim. Biophys. Acta. Biomembr. |
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10 |
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25 |
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1 |
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1863 |
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Biochimica et Biophysica Acta - Biomembranes |
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http://creativecommons.org/licenses/by-nc-nd/2.5/co/ |
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Elsevier |
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Ámsterdam, Países Bajos |
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Manrique Moreno, Marcela MaríaFandino Devia, Liliana EstefaníaPatino González, Edwin BaironSuwalsky, MarioJemioła Rzeminska, MałgorzataGrupo de Bioquímica Estructural de Macromoléculas2023-06-01T15:45:08Z2023-06-01T15:45:08Z2021Manrique-Moreno M, Suwalsky M, Patiño-González E, Fandiño-Devia E, Jemioła-Rzemińska M, Strzałka K. Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular models. Biochim Biophys Acta Biomembr. 2021 Feb 1;1863(2):183498. doi: 10.1016/j.bbamem.2020.183498.0005-2736https://hdl.handle.net/10495/3523210.1016/j.bbamem.2020.1834981879-2642ABSTRACT: Staphylococcus aureus is one of the most pathogenic bacteria; infections with it are associated with significant morbidity and mortality in health care facilities. Antimicrobial peptides are a promising next generation antibiotic with great potential against bacterial infections. In this study, evidence is presented of the biological and biophysical properties of the novel synthetic peptide ΔM3. Its antimicrobial activity against the ATCC 25923 and methicillin-resistant S. aureus strains was evaluated. The results showed that ΔM3 has activity in the same μM range as vancomycin. Biophysical studies were performed with palmitoyloleoylphosphatidylglycerol and cardiolipin liposomes loaded with calcein and used to follow the lytic activity of the peptide by fluorescence spectroscopy. On the other hand, ΔM3 was induced to interact with molecular models of the erythrocyte membrane buil-up of dimiristoylphosphatidylcholine and dimyristoylphosphatidylethanolamine, representative lipids of the outer and inner monolayers of the human erythrocyte membrane, respectively. The capacity of ΔM3 to interact with the bacteria and erythrocyte model membranes was also evaluated by X-ray diffraction and differential scanning calorimetry. The morphological changes induced by the peptide to human erythrocytes were observed by scanning electron microscopy. Results with these techniques indicated that ΔM3 interacted with the inner monolayer of the erythrocyte membrane, which is rich in anionic lipids. Additionally, the cytotoxic effects of ΔM3 on red blood cells were evaluated by monitoring the hemoglobin release from erythrocytes. The results obtained from these different approaches showed ΔM3 to be a non-cytotoxic peptide with antibacterial activityCOL015627510application/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_abf2Interaction of the antimicrobial peptide ∆M3 with the Staphylococcus aureus membrane and molecular modelsArtículo de investigaciónhttp://purl.org/coar/resource_type/c_2df8fbb1https://purl.org/redcol/resource_type/ARThttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionStaphylococcus aureusModelos MolecularesModels, MolecularMembrana celularCell MembranePéptidos catiónicos antimicrobianosAntimicrobial Cationic PeptidesBicapas lipídicasLipid BilayersBiochim. Biophys. Acta. 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