Study of the membrane activity of the synthetic peptide ∆M3 against extended-spectrum β-lactamase escherichia coli Isolates

ABSTRACT: Escherichia coli is the most common microorganism causing nosocomial or community-acquired bacteremia, and extended spectrum β-lactamase-producing Escherichia coli isolates are identifed worldwide with increasing frequency. For this reason, it is necessary to evaluate potential new molecul...

Full description

Autores:
Fandiño Devia, Liliana Estefanía
Santa González, Gloria Angelica
Klaiss Luna, María Camila
Manrique Moreno, Marcela María
Tipo de recurso:
Article of investigation
Fecha de publicación:
2024
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
eng
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/38087
Acceso en línea:
https://hdl.handle.net/10495/38087
Palabra clave:
Péptidos Antimicrobianos
Antimicrobial Peptides
Farmacorresistencia Microbiana
Drug Resistance, Microbial
Microscopía Fluorescente
Microscopy, Fluorescence
Espectroscopia de infrarrojos
Infrared spectroscopy
Extended-spectrum β-lactamase-producing in Escherichia coli
https://id.nlm.nih.gov/mesh/D000089882
https://id.nlm.nih.gov/mesh/D004352
https://id.nlm.nih.gov/mesh/D008856
Rights
openAccess
License
http://creativecommons.org/licenses/by/2.5/co/
id UDEA2_ec3acf4f11e28a26b6bee6687158954e
oai_identifier_str oai:bibliotecadigital.udea.edu.co:10495/38087
network_acronym_str UDEA2
network_name_str Repositorio UdeA
repository_id_str
dc.title.spa.fl_str_mv Study of the membrane activity of the synthetic peptide ∆M3 against extended-spectrum β-lactamase escherichia coli Isolates
title Study of the membrane activity of the synthetic peptide ∆M3 against extended-spectrum β-lactamase escherichia coli Isolates
spellingShingle Study of the membrane activity of the synthetic peptide ∆M3 against extended-spectrum β-lactamase escherichia coli Isolates
Péptidos Antimicrobianos
Antimicrobial Peptides
Farmacorresistencia Microbiana
Drug Resistance, Microbial
Microscopía Fluorescente
Microscopy, Fluorescence
Espectroscopia de infrarrojos
Infrared spectroscopy
Extended-spectrum β-lactamase-producing in Escherichia coli
https://id.nlm.nih.gov/mesh/D000089882
https://id.nlm.nih.gov/mesh/D004352
https://id.nlm.nih.gov/mesh/D008856
title_short Study of the membrane activity of the synthetic peptide ∆M3 against extended-spectrum β-lactamase escherichia coli Isolates
title_full Study of the membrane activity of the synthetic peptide ∆M3 against extended-spectrum β-lactamase escherichia coli Isolates
title_fullStr Study of the membrane activity of the synthetic peptide ∆M3 against extended-spectrum β-lactamase escherichia coli Isolates
title_full_unstemmed Study of the membrane activity of the synthetic peptide ∆M3 against extended-spectrum β-lactamase escherichia coli Isolates
title_sort Study of the membrane activity of the synthetic peptide ∆M3 against extended-spectrum β-lactamase escherichia coli Isolates
dc.creator.fl_str_mv Fandiño Devia, Liliana Estefanía
Santa González, Gloria Angelica
Klaiss Luna, María Camila
Manrique Moreno, Marcela María
dc.contributor.author.none.fl_str_mv Fandiño Devia, Liliana Estefanía
Santa González, Gloria Angelica
Klaiss Luna, María Camila
Manrique Moreno, Marcela María
dc.contributor.researchgroup.spa.fl_str_mv Grupo de Bioquímica Estructural de Macromoléculas
dc.subject.decs.none.fl_str_mv Péptidos Antimicrobianos
Antimicrobial Peptides
Farmacorresistencia Microbiana
Drug Resistance, Microbial
Microscopía Fluorescente
Microscopy, Fluorescence
topic Péptidos Antimicrobianos
Antimicrobial Peptides
Farmacorresistencia Microbiana
Drug Resistance, Microbial
Microscopía Fluorescente
Microscopy, Fluorescence
Espectroscopia de infrarrojos
Infrared spectroscopy
Extended-spectrum β-lactamase-producing in Escherichia coli
https://id.nlm.nih.gov/mesh/D000089882
https://id.nlm.nih.gov/mesh/D004352
https://id.nlm.nih.gov/mesh/D008856
dc.subject.lemb.none.fl_str_mv Espectroscopia de infrarrojos
Infrared spectroscopy
dc.subject.proposal.spa.fl_str_mv Extended-spectrum β-lactamase-producing in Escherichia coli
dc.subject.meshuri.none.fl_str_mv https://id.nlm.nih.gov/mesh/D000089882
https://id.nlm.nih.gov/mesh/D004352
https://id.nlm.nih.gov/mesh/D008856
description ABSTRACT: Escherichia coli is the most common microorganism causing nosocomial or community-acquired bacteremia, and extended spectrum β-lactamase-producing Escherichia coli isolates are identifed worldwide with increasing frequency. For this reason, it is necessary to evaluate potential new molecules like antimicrobial peptides. They are recognized for their biological potential which makes them promising candidates in the fght against infections. The goal of this research was to evaluate the potential of the synthetic peptide ΔM3 on several extended-spectrum β-lactamase producing E. coli isolates. The antimicrobial and cytotoxic activity of the peptide was spectrophotometrically determined. Additionally, the capacity of the peptide to interact with the bacterial membrane was monitored by fuorescence microscopy and infrared spectroscopy. The results demonstrated that the synthetic peptide is active against Escherichia coli isolates at concentrations similar to Meropenem. On the other hand, no cytotoxic efect was observed in HaCaT keratinocyte cells even at 10 times the minimal inhibitory concentration. Microscopy results showed a permeabilizing efect of the peptide on the bacteria. The infrared results showed that ΔM3 showed afnity for the lipids of the microorganism’s membrane. The results suggest that the ∆M3 interacts with the negatively charged lipids from the E. coli by a disturbing efect on membrane. Finally, the secondary structure experiments of the peptide showed a random structure in solution that did not change during the interaction with the membranes.
publishDate 2024
dc.date.accessioned.none.fl_str_mv 2024-02-07T21:26:17Z
dc.date.available.none.fl_str_mv 2024-02-07T21:26:17Z
dc.date.issued.none.fl_str_mv 2024
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 Fandiño-Devia, E., Santa-González, G.A., Klaiss-Luna, M.C. et al. Study of the Membrane Activity of the Synthetic Peptide ∆M3 Against Extended-Spectrum β-lactamase Escherichia coli Isolates. J Membrane Biol (2024). https://doi.org/10.1007/s00232-024-00306-3
dc.identifier.issn.none.fl_str_mv 0022-2631
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/10495/38087
dc.identifier.doi.none.fl_str_mv 10.1007/s00232-024-00306-3
dc.identifier.eissn.none.fl_str_mv 1432-1424
identifier_str_mv Fandiño-Devia, E., Santa-González, G.A., Klaiss-Luna, M.C. et al. Study of the Membrane Activity of the Synthetic Peptide ∆M3 Against Extended-Spectrum β-lactamase Escherichia coli Isolates. J Membrane Biol (2024). https://doi.org/10.1007/s00232-024-00306-3
0022-2631
10.1007/s00232-024-00306-3
1432-1424
url https://hdl.handle.net/10495/38087
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.ispartofjournalabbrev.spa.fl_str_mv J. Membr. Biol.
dc.relation.citationendpage.spa.fl_str_mv 11
dc.relation.citationstartpage.spa.fl_str_mv 1
dc.relation.ispartofjournal.spa.fl_str_mv Journal of Membrane Biology
dc.rights.uri.*.fl_str_mv http://creativecommons.org/licenses/by/2.5/co/
dc.rights.uri.spa.fl_str_mv https://creativecommons.org/licenses/by/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/2.5/co/
https://creativecommons.org/licenses/by/4.0/
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.extent.spa.fl_str_mv 11
dc.format.mimetype.spa.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Springer
dc.publisher.place.spa.fl_str_mv Nueva York, Estados Unidos
institution Universidad de Antioquia
bitstream.url.fl_str_mv https://bibliotecadigital.udea.edu.co/bitstreams/6529659c-689a-44b0-8bfb-59c6b4b7e33a/download
https://bibliotecadigital.udea.edu.co/bitstreams/ec6e6d5a-71a0-4eb3-9100-333c0c1893ac/download
https://bibliotecadigital.udea.edu.co/bitstreams/5173af27-bc95-4d78-9031-00534c4e80a2/download
https://bibliotecadigital.udea.edu.co/bitstreams/2a89fe3e-d8bf-4767-8b99-75a755d35d60/download
https://bibliotecadigital.udea.edu.co/bitstreams/045ed430-7d5c-4c5e-b860-715f31095b5c/download
bitstream.checksum.fl_str_mv ea7c99eb70b096fa987fca88201ef9a1
1646d1f6b96dbbbc38035efc9239ac9c
8a4605be74aa9ea9d79846c1fba20a33
dddcde24f0cb94b70fd4ba511720dc69
801f1a3e8c482f38c16a06bbee714414
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_ 1851052345466552320
spelling Fandiño Devia, Liliana EstefaníaSanta González, Gloria AngelicaKlaiss Luna, María CamilaManrique Moreno, Marcela MaríaGrupo de Bioquímica Estructural de Macromoléculas2024-02-07T21:26:17Z2024-02-07T21:26:17Z2024Fandiño-Devia, E., Santa-González, G.A., Klaiss-Luna, M.C. et al. Study of the Membrane Activity of the Synthetic Peptide ∆M3 Against Extended-Spectrum β-lactamase Escherichia coli Isolates. J Membrane Biol (2024). https://doi.org/10.1007/s00232-024-00306-30022-2631https://hdl.handle.net/10495/3808710.1007/s00232-024-00306-31432-1424ABSTRACT: Escherichia coli is the most common microorganism causing nosocomial or community-acquired bacteremia, and extended spectrum β-lactamase-producing Escherichia coli isolates are identifed worldwide with increasing frequency. For this reason, it is necessary to evaluate potential new molecules like antimicrobial peptides. They are recognized for their biological potential which makes them promising candidates in the fght against infections. The goal of this research was to evaluate the potential of the synthetic peptide ΔM3 on several extended-spectrum β-lactamase producing E. coli isolates. The antimicrobial and cytotoxic activity of the peptide was spectrophotometrically determined. Additionally, the capacity of the peptide to interact with the bacterial membrane was monitored by fuorescence microscopy and infrared spectroscopy. The results demonstrated that the synthetic peptide is active against Escherichia coli isolates at concentrations similar to Meropenem. On the other hand, no cytotoxic efect was observed in HaCaT keratinocyte cells even at 10 times the minimal inhibitory concentration. Microscopy results showed a permeabilizing efect of the peptide on the bacteria. The infrared results showed that ΔM3 showed afnity for the lipids of the microorganism’s membrane. The results suggest that the ∆M3 interacts with the negatively charged lipids from the E. coli by a disturbing efect on membrane. Finally, the secondary structure experiments of the peptide showed a random structure in solution that did not change during the interaction with the membranes.COL015627511application/pdfengSpringerNueva York, Estados Unidoshttp://creativecommons.org/licenses/by/2.5/co/https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Study of the membrane activity of the synthetic peptide ∆M3 against extended-spectrum β-lactamase escherichia coli IsolatesArtículo 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/publishedVersionPéptidos AntimicrobianosAntimicrobial PeptidesFarmacorresistencia MicrobianaDrug Resistance, MicrobialMicroscopía FluorescenteMicroscopy, FluorescenceEspectroscopia de infrarrojosInfrared spectroscopyExtended-spectrum β-lactamase-producing in Escherichia colihttps://id.nlm.nih.gov/mesh/D000089882https://id.nlm.nih.gov/mesh/D004352https://id.nlm.nih.gov/mesh/D008856J. Membr. Biol.111Journal of Membrane BiologyPublicationORIGINALFandiñoEstefania_2024_StudyMembraneActivity.pdfFandiñoEstefania_2024_StudyMembraneActivity.pdfArtículo de investigaciónapplication/pdf2166059https://bibliotecadigital.udea.edu.co/bitstreams/6529659c-689a-44b0-8bfb-59c6b4b7e33a/downloadea7c99eb70b096fa987fca88201ef9a1MD51trueAnonymousREADCC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8927https://bibliotecadigital.udea.edu.co/bitstreams/ec6e6d5a-71a0-4eb3-9100-333c0c1893ac/download1646d1f6b96dbbbc38035efc9239ac9cMD52falseAnonymousREADLICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://bibliotecadigital.udea.edu.co/bitstreams/5173af27-bc95-4d78-9031-00534c4e80a2/download8a4605be74aa9ea9d79846c1fba20a33MD53falseAnonymousREADTEXTFandiñoEstefania_2024_StudyMembraneActivity.pdf.txtFandiñoEstefania_2024_StudyMembraneActivity.pdf.txtExtracted texttext/plain55832https://bibliotecadigital.udea.edu.co/bitstreams/2a89fe3e-d8bf-4767-8b99-75a755d35d60/downloaddddcde24f0cb94b70fd4ba511720dc69MD54falseAnonymousREADTHUMBNAILFandiñoEstefania_2024_StudyMembraneActivity.pdf.jpgFandiñoEstefania_2024_StudyMembraneActivity.pdf.jpgGenerated Thumbnailimage/jpeg12590https://bibliotecadigital.udea.edu.co/bitstreams/045ed430-7d5c-4c5e-b860-715f31095b5c/download801f1a3e8c482f38c16a06bbee714414MD55falseAnonymousREAD10495/38087oai:bibliotecadigital.udea.edu.co:10495/380872025-03-26 20:55:23.462http://creativecommons.org/licenses/by/2.5/co/open.accesshttps://bibliotecadigital.udea.edu.coRepositorio Institucional de la Universidad de Antioquiaaplicacionbibliotecadigitalbiblioteca@udea.edu.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