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...

Full description

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/
id UDEA2_5b499976a934a434ea2bcccc3c246ab2
oai_identifier_str oai:bibliotecadigital.udea.edu.co:10495/35232
network_acronym_str UDEA2
network_name_str Repositorio UdeA
repository_id_str
dc.title.spa.fl_str_mv 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
dc.type.coar.spa.fl_str_mv http://purl.org/coar/resource_type/c_2df8fbb1
dc.type.redcol.spa.fl_str_mv https://purl.org/redcol/resource_type/ART
dc.type.coarversion.spa.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.driver.spa.fl_str_mv info:eu-repo/semantics/article
dc.type.version.spa.fl_str_mv info:eu-repo/semantics/publishedVersion
format http://purl.org/coar/resource_type/c_2df8fbb1
status_str publishedVersion
dc.identifier.citation.spa.fl_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.
dc.identifier.issn.none.fl_str_mv 0005-2736
dc.identifier.uri.none.fl_str_mv 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
dc.relation.ispartofjournalabbrev.spa.fl_str_mv Biochim. Biophys. Acta. Biomembr.
dc.relation.citationendpage.spa.fl_str_mv 10
dc.relation.citationissue.spa.fl_str_mv 25
dc.relation.citationstartpage.spa.fl_str_mv 1
dc.relation.citationvolume.spa.fl_str_mv 1863
dc.relation.ispartofjournal.spa.fl_str_mv Biochimica et Biophysica Acta - Biomembranes
dc.rights.uri.*.fl_str_mv http://creativecommons.org/licenses/by-nc-nd/2.5/co/
dc.rights.uri.spa.fl_str_mv https://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.accessrights.spa.fl_str_mv info:eu-repo/semantics/openAccess
dc.rights.coar.spa.fl_str_mv http://purl.org/coar/access_right/c_abf2
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/2.5/co/
https://creativecommons.org/licenses/by-nc-nd/4.0/
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.extent.spa.fl_str_mv 10
dc.format.mimetype.spa.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Elsevier
dc.publisher.place.spa.fl_str_mv Ámsterdam, Países Bajos
institution Universidad de Antioquia
bitstream.url.fl_str_mv https://bibliotecadigital.udea.edu.co/bitstreams/7a2fbf3c-5f27-4f4d-9b66-d673fa351384/download
https://bibliotecadigital.udea.edu.co/bitstreams/016a0cb7-64fb-401a-b8e4-15e4419537b0/download
https://bibliotecadigital.udea.edu.co/bitstreams/50f9563a-ebc0-448c-99e1-c3b1bed3862b/download
https://bibliotecadigital.udea.edu.co/bitstreams/834d1d7d-2519-4ae8-b14e-fbe8ddb5bd69/download
https://bibliotecadigital.udea.edu.co/bitstreams/64007053-def9-41fd-af4d-d2b3b20e4058/download
bitstream.checksum.fl_str_mv 6afef6ad461eff99af3d4ab5b33604fa
b88b088d9957e670ce3b3fbe2eedbc13
8a4605be74aa9ea9d79846c1fba20a33
98c73e677f51c92b01cae2e9feabe15b
401e6bcdd95cfff17fc09269eac03240
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
MD5
MD5
MD5
repository.name.fl_str_mv Repositorio Institucional de la Universidad de Antioquia
repository.mail.fl_str_mv aplicacionbibliotecadigitalbiblioteca@udea.edu.co
_version_ 1851052175519645696
spelling 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. Biomembr.102511863Biochimica et Biophysica Acta - BiomembranesPublicationORIGINALManriqueMarcela_2020_InteractionAntimicrobialPeptide.pdfManriqueMarcela_2020_InteractionAntimicrobialPeptide.pdfArtículo de investigaciónapplication/pdf1791384https://bibliotecadigital.udea.edu.co/bitstreams/7a2fbf3c-5f27-4f4d-9b66-d673fa351384/download6afef6ad461eff99af3d4ab5b33604faMD51trueAnonymousREADCC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8823https://bibliotecadigital.udea.edu.co/bitstreams/016a0cb7-64fb-401a-b8e4-15e4419537b0/downloadb88b088d9957e670ce3b3fbe2eedbc13MD52falseAnonymousREADLICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://bibliotecadigital.udea.edu.co/bitstreams/50f9563a-ebc0-448c-99e1-c3b1bed3862b/download8a4605be74aa9ea9d79846c1fba20a33MD53falseAnonymousREADTEXTManriqueMarcela_2020_InteractionAntimicrobialPeptide.pdf.txtManriqueMarcela_2020_InteractionAntimicrobialPeptide.pdf.txtExtracted texttext/plain73645https://bibliotecadigital.udea.edu.co/bitstreams/834d1d7d-2519-4ae8-b14e-fbe8ddb5bd69/download98c73e677f51c92b01cae2e9feabe15bMD56falseAnonymousREADTHUMBNAILManriqueMarcela_2020_InteractionAntimicrobialPeptide.pdf.jpgManriqueMarcela_2020_InteractionAntimicrobialPeptide.pdf.jpgGenerated Thumbnailimage/jpeg14276https://bibliotecadigital.udea.edu.co/bitstreams/64007053-def9-41fd-af4d-d2b3b20e4058/download401e6bcdd95cfff17fc09269eac03240MD57falseAnonymousREAD10495/35232oai:bibliotecadigital.udea.edu.co:10495/352322025-03-26 18:08:11.326http://creativecommons.org/licenses/by-nc-nd/2.5/co/open.accesshttps://bibliotecadigital.udea.edu.coRepositorio Institucional de la Universidad de Antioquiaaplicacionbibliotecadigitalbiblioteca@udea.edu.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