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...
- 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/
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| 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 |
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https://purl.org/redcol/resource_type/ART |
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http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| dc.type.driver.spa.fl_str_mv |
info:eu-repo/semantics/article |
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info:eu-repo/semantics/publishedVersion |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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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/ |
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info:eu-repo/semantics/openAccess |
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http://creativecommons.org/licenses/by/2.5/co/ https://creativecommons.org/licenses/by/4.0/ http://purl.org/coar/access_right/c_abf2 |
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openAccess |
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application/pdf |
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Springer |
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Nueva York, Estados Unidos |
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Universidad de Antioquia |
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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. 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