Caracterización de la actividad lítica de lipopéptidos cíclicos producidos por Bacillus velezencis en sistemas modelo de membranas de Pseudomonas aeruginosa y eritrocitos.
Tesis de grado para obtener el título de físico.
- Autores:
-
Cabrera Jojoa, Ángela Carolina
- Tipo de recurso:
- Trabajo de grado de pregrado
- Fecha de publicación:
- 2024
- Institución:
- Universidad de los Andes
- Repositorio:
- Séneca: repositorio Uniandes
- Idioma:
- spa
- OAI Identifier:
- oai:repositorio.uniandes.edu.co:1992/74989
- Acceso en línea:
- https://hdl.handle.net/1992/74989
- Palabra clave:
- Resistencia a antibióticos
Lipopéptidos cíclicos
Bacillus velezensis
Modelos de membrana
Pseudomonas aeruginosa
Eritrocitos
Lisis celular
Anisotropía
Estructura de la membrana
Fengicinas
Péptidos Antimicrobianos
Fluidez de membrana
Física
- Rights
- openAccess
- License
- Attribution-NonCommercial-NoDerivatives 4.0 International
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dc.title.spa.fl_str_mv |
Caracterización de la actividad lítica de lipopéptidos cíclicos producidos por Bacillus velezencis en sistemas modelo de membranas de Pseudomonas aeruginosa y eritrocitos. |
title |
Caracterización de la actividad lítica de lipopéptidos cíclicos producidos por Bacillus velezencis en sistemas modelo de membranas de Pseudomonas aeruginosa y eritrocitos. |
spellingShingle |
Caracterización de la actividad lítica de lipopéptidos cíclicos producidos por Bacillus velezencis en sistemas modelo de membranas de Pseudomonas aeruginosa y eritrocitos. Resistencia a antibióticos Lipopéptidos cíclicos Bacillus velezensis Modelos de membrana Pseudomonas aeruginosa Eritrocitos Lisis celular Anisotropía Estructura de la membrana Fengicinas Péptidos Antimicrobianos Fluidez de membrana Física |
title_short |
Caracterización de la actividad lítica de lipopéptidos cíclicos producidos por Bacillus velezencis en sistemas modelo de membranas de Pseudomonas aeruginosa y eritrocitos. |
title_full |
Caracterización de la actividad lítica de lipopéptidos cíclicos producidos por Bacillus velezencis en sistemas modelo de membranas de Pseudomonas aeruginosa y eritrocitos. |
title_fullStr |
Caracterización de la actividad lítica de lipopéptidos cíclicos producidos por Bacillus velezencis en sistemas modelo de membranas de Pseudomonas aeruginosa y eritrocitos. |
title_full_unstemmed |
Caracterización de la actividad lítica de lipopéptidos cíclicos producidos por Bacillus velezencis en sistemas modelo de membranas de Pseudomonas aeruginosa y eritrocitos. |
title_sort |
Caracterización de la actividad lítica de lipopéptidos cíclicos producidos por Bacillus velezencis en sistemas modelo de membranas de Pseudomonas aeruginosa y eritrocitos. |
dc.creator.fl_str_mv |
Cabrera Jojoa, Ángela Carolina |
dc.contributor.advisor.none.fl_str_mv |
Leidy, Chad Medeot, Daniela Beatriz |
dc.contributor.author.none.fl_str_mv |
Cabrera Jojoa, Ángela Carolina |
dc.contributor.jury.none.fl_str_mv |
Forero Shelton, Antonio Manu |
dc.contributor.researchgroup.none.fl_str_mv |
Facultad de Ciencias::Biofísica |
dc.subject.keyword.spa.fl_str_mv |
Resistencia a antibióticos Lipopéptidos cíclicos Bacillus velezensis Modelos de membrana Pseudomonas aeruginosa Eritrocitos Lisis celular Anisotropía Estructura de la membrana Fengicinas Péptidos Antimicrobianos Fluidez de membrana |
topic |
Resistencia a antibióticos Lipopéptidos cíclicos Bacillus velezensis Modelos de membrana Pseudomonas aeruginosa Eritrocitos Lisis celular Anisotropía Estructura de la membrana Fengicinas Péptidos Antimicrobianos Fluidez de membrana Física |
dc.subject.themes.spa.fl_str_mv |
Física |
description |
Tesis de grado para obtener el título de físico. |
publishDate |
2024 |
dc.date.accessioned.none.fl_str_mv |
2024-08-05T16:35:58Z |
dc.date.available.none.fl_str_mv |
2024-08-05T16:35:58Z |
dc.date.issued.none.fl_str_mv |
2024-05-31 |
dc.type.none.fl_str_mv |
Trabajo de grado - Pregrado |
dc.type.driver.none.fl_str_mv |
info:eu-repo/semantics/bachelorThesis |
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info:eu-repo/semantics/acceptedVersion |
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http://purl.org/coar/resource_type/c_7a1f |
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http://purl.org/redcol/resource_type/TP |
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dc.identifier.uri.none.fl_str_mv |
https://hdl.handle.net/1992/74989 |
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instname:Universidad de los Andes |
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reponame:Repositorio Institucional Séneca |
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repourl:https://repositorio.uniandes.edu.co/ |
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instname:Universidad de los Andes reponame:Repositorio Institucional Séneca repourl:https://repositorio.uniandes.edu.co/ |
dc.language.iso.none.fl_str_mv |
spa |
language |
spa |
dc.relation.references.none.fl_str_mv |
1. O’Neill, J. Tackling drug-resistant infections globally: final report and recommendations (2016). 2. Organización Mundial de la Salud. OMS publica lista de bacterias para las cuales se necesitan con urgencia nuevos antibióticos https://www.who.int/es/news/item/27-02-2017-who-publishes-list-of-bacteria-for-which-new-antibiotics-are-urgentlyneeded. Consultado el 1 de abril de 2024. 2017. 3. Marín-Medina, N., Ramírez, D. A., Trier, S. y Leidy, C. Mechanical properties that influence antimicrobial peptide activity in lipid membranes. Applied microbiology and biotechnology 100, 10251-10263 (2016). 4. Roque-Borda, C. A. et al. Challenge in the discovery of new drugs: antimicrobial peptides against WHO-list of critical and high-priority bacteria. Pharmaceutics 13, 773 (2021). 5. Hamley, I. W. Lipopeptides: from self-assembly to bioactivity. Chemical Communications 51, 8574-8583 (2015). 6. Rubio, S., Martínez-Cámara, S., de la Fuente, J. L., Rodríguez-Sáiz, M. y Barredo, J.-L. en Antimicrobial Therapies: Methods and Protocols 351-363 (Springer, 2021). 7. Ball, L.-J., Goult, C. M., Donarski, J. A., Micklefield, J. y Ramesh, V. NMR structure determination and calcium binding effects of lipopeptide antibiotic daptomycin. Organic & biomolecular chemistry 2, 1872-1878 (2004). 8. Fira, D., Dimkić, I., Berić, T., Lozo, J. y Stanković, S. Biological control of plant pathogens by Bacillus species. Journal of biotechnology 285, 44-55 (2018). 9. Fan, H. Y. et al. Utilizing zeta potential measurements to study the effective charge, membrane partitioning, and membrane permeation of the lipopeptide surfactin. en. Biochimica et Biophysica Acta (BBA) - Biomembranes 1838, 2306-2312. issn: 00052736. https://linkinghub.elsevier.com/retrieve/pii/S0005273614000820 (2023) (sep. de 2014). 10. Heerklotz, H. y Seelig, J. Leakage and lysis of lipid membranes induced by the lipopeptide surfactin. en. European Biophysics Journal 36, 305-314. issn: 0175-7571, 1432-1017. https://link.springer.com/10.1007/s00249-006-0091-5 (2023) (abr. de 2007). 11. Jiang, C. et al. Bacillus subtilis inhibits Aspergillus carbonarius by producing iturin A, which disturbs the transport, energy metabolism, and osmotic pressure of fungal cells as revealed by transcriptomics analysis. International journal of food microbiology 330, 108783 (2020). 12. Akpa, E. et al. Influence of Culture Conditions on Lipopeptide Production by Bacillus subtilis. en. Applied Biochemistry and Biotechnology 91-93, 551-562. issn: 0273-2289. http://link.springer.com/10.1385/ABAB:91-93:1-9:551 (2023) (2001). 13. Bie, X., Lu, Z. y Lu, F. Identification of fengycin homologues from Bacillus subtilis with ESI-MS/CID. en. Journal of Microbiological Methods 79, 272-278. issn: 01677012. https://linkinghub.elsevier.com/retrieve/pii/S0167701209002978 (2023) (dic. de 2009). 14. Medeot, D. B., Fernandez, M., Morales, G. M. y Jofré, E. Fengycins From Bacillus amyloliquefaciens MEP218 Exhibit Antibacterial Activity by Producing Alterations on the Cell Surface of the Pathogens Xanthomonas axonopodis pv. vesicatoria and Pseudomonas aeruginosa PA01. Frontiers in Microbiology 10, 3107. issn: 1664-302X. https://www.frontiersin.org/article/10.3389/fmicb.2019.03107/full (2023) (ene. de 2020). 15. Sur, S., Romo, T. D. y Grossfield, A. Selectivity and Mechanism of Fengycin, an Antimicrobial Lipopeptide, from Molecular Dynamics. en. The Journal of Physical Chemistry B 122, 2219-2226. issn: 1520-6106, 1520-5207. https://pubs.acs.org/doi/10.1021/acs.jpcb.7b11889 (2023) (mar. de 2018). 16. Strahl, H. y Errington, J. Bacterial Membranes: Structure, Domains, and Function. en. Annual Review of Microbiology 71, 519-538. issn: 0066-4227, 1545-3251. https://www.annualreviews.org/doi/10.1146/annurev-micro-102215-095630 (2024) (sep. de 2017). 17. Bagatolli, L. Vida ¿una cuestión de grasas?: una perspectiva desde la biofísica de membranas spa. OCLC: 1026126232. isbn: 978-9942-07-694-6 (El Telégrafo, Quito, 2014). 18. Bagatolli, L.A., Ipsen, J. H., Simonsen,A. C. y Mouritsen, O. G.Anoutlook on organization of lipids in membranes: searching for a realistic connection with the organization of biological membranes. Progress in lipid research 49, 378-389 (2010). 19. Van Oss, C. J. Hydrophobicity and hydrophilicity of biosurfaces. Current opinion in colloid & interface science 2, 503-512 (1997). 20. Lochab, V. et al. Ultrastructure imaging of Pseudomonas aeruginosa lawn biofilms and eradication of the tobramycin-resistant variants under in vitro electroceutical treatment. Scientific reports 10, 9879 (2020). 21. Meisenberg, G. y Simmons,W. H. Principles of Medical Biochemistry E-Book: Principles of Medical Biochemistry E-Book (Elsevier Health Sciences, 2016). 22. Joensuu, M., Wallis, T. P., Saber, S. H. y Meunier, F. A. Phospholipases in neuronal function: A role in learning and memory? Journal of neurochemistry 153, 300-333 (2020). 23. Nelson, D. L., Lehninger,A. L. y Cox, M. M. Lehninger principles of biochemistry (Macmillan, 2008). 24. Gesto, D. S., Pereira, C. M., Cerqueira, N. M. y Sousa, S. F. An atomic-level perspective of HMG-CoA-reductase: The target enzyme to treat hypercholesterolemia. Molecules 25, 3891 (2020). 25. Bartholomew, J.W. y Mittwer, T. The gram stain. Bacteriological reviews 16, 1-29 (1952). 26. Burton, G. R.W. Microbiology for the health sciences. (No Title) (2000). 27. Royer, C. A. Fluorescence spectroscopy. Protein stability and folding: Theory and practice, 65-89 (1995). 28. Maherani, B., Arab-Tehrany, E., Kheirolomoom, A., Geny, D. y Linder, M. Calcein release behavior from liposomal bilayer; influence of physicochemical/mechanical/structural properties of lipids. Biochimie 95, 2018-2033 (2013). 29. Kuhry, J.-G., Fonteneau, P., Duportail, G., Maechling, C. y Laustriat, G. TMA-DPH: a suitable fluorescence polarization probe for specific plasma membrane fluidity studies in intact living cells. Cell biophysics 5, 129-140 (1983). 30. Calderón-Rivera, N. et al. Cardiolipin Strongly Inhibits the Leakage Activity of the Short Antimicrobial Peptide ATRA-1 in Comparison to LL-37, in Model Membranes Mimicking the Lipid Composition of Staphylococcus aureus. en. Membranes 13, 304. issn: 2077-0375. https://www.mdpi.com/2077-0375/13/3/304 (2023) (mar. de 2023). 31. Rivera-Sanchez, S. P. et al. Integrating In Vitro and In Silico Analysis of a Cationic Antimicrobial Peptide Interaction with Model Membranes of Colistin-Resistant Pseudomonas aeruginosa Strains. en. Pharmaceutics 14, 1248. issn: 1999-4923. https://www.mdpi.com/1999-4923/14/6/1248 (2023) (jun. de 2022). 32. Bali, R. et al. Macroscopic domain formation during cooling in the platelet plasma membrane: An issue of low cholesterol content. en. Biochimica et Biophysica Acta (BBA) - Biomembranes 1788, 1229-1237. issn: 00052736. https://linkinghub.elsevier.com/retrieve/pii/S000527360900100X (2023) (jun. de 2009). 33. Doktorova, M. et al. Cell membranes sustain phospholipid imbalance via cholesterol asymmetry. bioRxiv, 2023-07 (2023). 34. Alleva, K. y Federico, L. Análisis estructuralista de las teorías de Hill: una elucidación de explicación en bioquímica. Scientiae Studia 11, 333-353 (2013) 35. Grau-Campistany, A., Manresa, A., Pujol, M., Rabanal, F. y Cajal, Y. Tryptophancontaining lipopeptide antibiotics derived from polymyxin B with activity against Gram positive and Gram negative bacteria. Biochimica et Biophysica Acta (BBA)-Biomembranes 1858, 333-343 (2016). 36. Koller, D. y Lohner, K. The role of spontaneous lipid curvature in the interaction of interfacially active peptides with membranes. Biochimica et Biophysica Acta (BBA)-Biomembranes 1838, 2250-2259 (2014). 37. Heerklotz, H., Wieprecht, T. y Seelig, J. Membrane perturbation by the lipopeptide surfactin and detergents as studied by deuterium NMR. The Journal of Physical Chemistry B 108, 4909-4915 (2004). |
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Leidy, Chadvirtual::19590-1Medeot, Daniela BeatrizCabrera Jojoa, Ángela CarolinaForero Shelton, Antonio Manuvirtual::19591-1Facultad de Ciencias::Biofísica2024-08-05T16:35:58Z2024-08-05T16:35:58Z2024-05-31https://hdl.handle.net/1992/74989instname:Universidad de los Andesreponame:Repositorio Institucional Sénecarepourl:https://repositorio.uniandes.edu.co/Tesis de grado para obtener el título de físico.La constante lucha contra los organismos resistentes a antibióticos ha permitido explorar alternativas poco convencionales para hacerles frente, como buscar en la misma naturaleza moléculas que combatan a sus homólogos y permitan el control biológico. Este estudio evaluó la capacidad antibiótica de lipopéptidos cíclicos producidos por Bacillus velezensis. Se caracterizaron cambios en la membrana utilizando modelos de membrana de Pseudomonas aeruginosa y eritocitos, bajo mediciones de fuga de contenido y de anisotropía. Los resultados mostraron que los lipopéptidos totales inducen lisis celular, especialmente en membranas con reducido espaciamiento de cabezas polares y mayor densidad de carga superficial. La estructura y composición de la membrana influyen significativamente en la susceptibilidad a la lisis. El modelo de Pseudomonas aeruginosa mostró mayor resistencia comparado con los modelos POPC y POPG, con excepción de eritrocitos. Aunque los lipopéptidos totales son efectivos en el modelo de eritrocitos, presentan menor cooperatividad y requieren mayores concentraciones para inducir lisis en comparación con las fengicinas, las cuales tienen mayor cooperatividad y ventajas como potenciales antibióticos. La fluidez de la membrana de Pseudomonas aeruginosa, que incluye la molécula cónica PE, es menos sensible a los lipopéptidos totales en comparación con los modelos de moléculas cilíndricas POPC y POPG, posiblemente debido a la estructura cónica de PE que facilita la acomodación del lipopéptido entre las cabezas polares. Estos hallazgos sugieren que los lipopéptidos cíclicos (lipopétidos totales y fengicinas aisladas) producidos por Bacillus velezensis son una prometedora alternativa en el desarrollo de nuevos tratamientos antibacterianos, ofreciendo una solución potencial frente a la creciente amenaza de resistencia a los antibióticos.The ongoing battle against antibiotic-resistant organisms has led to exploring unconventional alternatives, such as searching within nature for molecules that combat their counterparts and enable biological control. This study evaluated the antibiotic capacity of cyclic lipopeptides produced by Bacillus velezensis. Membrane changes were characterized using membrane models of Pseudomonas aeruginosa and erythrocytes, under measurements of leakage and anisotropy. Results showed that total lipopeptides induce cell lysis, especially in membranes with reduced polar head spacing and higher surface charge density. Membrane structure and composition significantly influence susceptibility to lysis. The Pseudomonas aeruginosa model showed greater resistance concerning the POPC and POPG models, except erythrocytes. Although total lipopeptides are effective in the erythrocyte model, they exhibit lower cooperativity and require higher concentrations to induce lysis concerning fengycins, which have higher cooperativity and advantages as potential antibiotics. The membrane fluidity of Pseudomonas aeruginosa, which includes the conical molecule PE, is less sensitive to total lipopeptides compared to cylindrical molecule models POPC and POPG, possibly due to the conical structure of PE facilitating the accommodation of the lipopeptide among the polar heads. These findings suggest that lipopeptides (total lipopeptides and isolated fengycins) produced by Bacillus velezensis are a promising alternative in the development of new antibacterial treatments, offering a potential solution to the growing threat of antibiotic resistance.PregradoBiofísica de membranas39 páginasapplication/pdfspaUniversidad de los AndesFísicaFacultad de CienciasDepartamento de FísicaAttribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Caracterización de la actividad lítica de lipopéptidos cíclicos producidos por Bacillus velezencis en sistemas modelo de membranas de Pseudomonas aeruginosa y eritrocitos.Trabajo de grado - Pregradoinfo:eu-repo/semantics/bachelorThesisinfo:eu-repo/semantics/acceptedVersionhttp://purl.org/coar/resource_type/c_7a1fTexthttp://purl.org/redcol/resource_type/TPResistencia a antibióticosLipopéptidos cíclicosBacillus velezensisModelos de membranaPseudomonas aeruginosaEritrocitosLisis celularAnisotropíaEstructura de la membranaFengicinasPéptidos AntimicrobianosFluidez de membranaFísica1. O’Neill, J. Tackling drug-resistant infections globally: final report and recommendations (2016).2. Organización Mundial de la Salud. OMS publica lista de bacterias para las cuales se necesitan con urgencia nuevos antibióticos https://www.who.int/es/news/item/27-02-2017-who-publishes-list-of-bacteria-for-which-new-antibiotics-are-urgentlyneeded. Consultado el 1 de abril de 2024. 2017.3. Marín-Medina, N., Ramírez, D. A., Trier, S. y Leidy, C. Mechanical properties that influence antimicrobial peptide activity in lipid membranes. Applied microbiology and biotechnology 100, 10251-10263 (2016).4. Roque-Borda, C. A. et al. Challenge in the discovery of new drugs: antimicrobial peptides against WHO-list of critical and high-priority bacteria. Pharmaceutics 13, 773 (2021).5. Hamley, I. W. Lipopeptides: from self-assembly to bioactivity. Chemical Communications 51, 8574-8583 (2015).6. Rubio, S., Martínez-Cámara, S., de la Fuente, J. L., Rodríguez-Sáiz, M. y Barredo, J.-L. en Antimicrobial Therapies: Methods and Protocols 351-363 (Springer, 2021).7. Ball, L.-J., Goult, C. M., Donarski, J. A., Micklefield, J. y Ramesh, V. NMR structure determination and calcium binding effects of lipopeptide antibiotic daptomycin. Organic & biomolecular chemistry 2, 1872-1878 (2004).8. Fira, D., Dimkić, I., Berić, T., Lozo, J. y Stanković, S. Biological control of plant pathogens by Bacillus species. Journal of biotechnology 285, 44-55 (2018).9. Fan, H. Y. et al. Utilizing zeta potential measurements to study the effective charge, membrane partitioning, and membrane permeation of the lipopeptide surfactin. en. Biochimica et Biophysica Acta (BBA) - Biomembranes 1838, 2306-2312. issn: 00052736. https://linkinghub.elsevier.com/retrieve/pii/S0005273614000820 (2023) (sep. de 2014).10. Heerklotz, H. y Seelig, J. Leakage and lysis of lipid membranes induced by the lipopeptide surfactin. en. European Biophysics Journal 36, 305-314. issn: 0175-7571, 1432-1017. https://link.springer.com/10.1007/s00249-006-0091-5 (2023) (abr. de 2007).11. Jiang, C. et al. Bacillus subtilis inhibits Aspergillus carbonarius by producing iturin A, which disturbs the transport, energy metabolism, and osmotic pressure of fungal cells as revealed by transcriptomics analysis. International journal of food microbiology 330, 108783 (2020).12. Akpa, E. et al. Influence of Culture Conditions on Lipopeptide Production by Bacillus subtilis. en. Applied Biochemistry and Biotechnology 91-93, 551-562. issn: 0273-2289. http://link.springer.com/10.1385/ABAB:91-93:1-9:551 (2023) (2001).13. Bie, X., Lu, Z. y Lu, F. Identification of fengycin homologues from Bacillus subtilis with ESI-MS/CID. en. Journal of Microbiological Methods 79, 272-278. issn: 01677012. https://linkinghub.elsevier.com/retrieve/pii/S0167701209002978 (2023) (dic. de 2009).14. Medeot, D. B., Fernandez, M., Morales, G. M. y Jofré, E. Fengycins From Bacillus amyloliquefaciens MEP218 Exhibit Antibacterial Activity by Producing Alterations on the Cell Surface of the Pathogens Xanthomonas axonopodis pv. vesicatoria and Pseudomonas aeruginosa PA01. Frontiers in Microbiology 10, 3107. issn: 1664-302X. https://www.frontiersin.org/article/10.3389/fmicb.2019.03107/full (2023) (ene. de 2020).15. Sur, S., Romo, T. D. y Grossfield, A. Selectivity and Mechanism of Fengycin, an Antimicrobial Lipopeptide, from Molecular Dynamics. en. The Journal of Physical Chemistry B 122, 2219-2226. issn: 1520-6106, 1520-5207. https://pubs.acs.org/doi/10.1021/acs.jpcb.7b11889 (2023) (mar. de 2018).16. Strahl, H. y Errington, J. Bacterial Membranes: Structure, Domains, and Function. en. Annual Review of Microbiology 71, 519-538. issn: 0066-4227, 1545-3251. https://www.annualreviews.org/doi/10.1146/annurev-micro-102215-095630 (2024) (sep. de 2017).17. Bagatolli, L. Vida ¿una cuestión de grasas?: una perspectiva desde la biofísica de membranas spa. OCLC: 1026126232. isbn: 978-9942-07-694-6 (El Telégrafo, Quito, 2014).18. Bagatolli, L.A., Ipsen, J. H., Simonsen,A. C. y Mouritsen, O. G.Anoutlook on organization of lipids in membranes: searching for a realistic connection with the organization of biological membranes. Progress in lipid research 49, 378-389 (2010).19. Van Oss, C. J. Hydrophobicity and hydrophilicity of biosurfaces. Current opinion in colloid & interface science 2, 503-512 (1997).20. Lochab, V. et al. Ultrastructure imaging of Pseudomonas aeruginosa lawn biofilms and eradication of the tobramycin-resistant variants under in vitro electroceutical treatment. Scientific reports 10, 9879 (2020).21. Meisenberg, G. y Simmons,W. H. Principles of Medical Biochemistry E-Book: Principles of Medical Biochemistry E-Book (Elsevier Health Sciences, 2016).22. Joensuu, M., Wallis, T. P., Saber, S. H. y Meunier, F. A. Phospholipases in neuronal function: A role in learning and memory? Journal of neurochemistry 153, 300-333 (2020).23. Nelson, D. L., Lehninger,A. L. y Cox, M. M. Lehninger principles of biochemistry (Macmillan, 2008).24. Gesto, D. S., Pereira, C. M., Cerqueira, N. M. y Sousa, S. F. An atomic-level perspective of HMG-CoA-reductase: The target enzyme to treat hypercholesterolemia. Molecules 25, 3891 (2020).25. Bartholomew, J.W. y Mittwer, T. The gram stain. Bacteriological reviews 16, 1-29 (1952).26. Burton, G. R.W. Microbiology for the health sciences. (No Title) (2000).27. Royer, C. A. Fluorescence spectroscopy. Protein stability and folding: Theory and practice, 65-89 (1995).28. Maherani, B., Arab-Tehrany, E., Kheirolomoom, A., Geny, D. y Linder, M. Calcein release behavior from liposomal bilayer; influence of physicochemical/mechanical/structural properties of lipids. Biochimie 95, 2018-2033 (2013).29. Kuhry, J.-G., Fonteneau, P., Duportail, G., Maechling, C. y Laustriat, G. TMA-DPH: a suitable fluorescence polarization probe for specific plasma membrane fluidity studies in intact living cells. Cell biophysics 5, 129-140 (1983).30. Calderón-Rivera, N. et al. Cardiolipin Strongly Inhibits the Leakage Activity of the Short Antimicrobial Peptide ATRA-1 in Comparison to LL-37, in Model Membranes Mimicking the Lipid Composition of Staphylococcus aureus. en. Membranes 13, 304. issn: 2077-0375. https://www.mdpi.com/2077-0375/13/3/304 (2023) (mar. de 2023).31. Rivera-Sanchez, S. P. et al. Integrating In Vitro and In Silico Analysis of a Cationic Antimicrobial Peptide Interaction with Model Membranes of Colistin-Resistant Pseudomonas aeruginosa Strains. en. Pharmaceutics 14, 1248. issn: 1999-4923. https://www.mdpi.com/1999-4923/14/6/1248 (2023) (jun. de 2022).32. Bali, R. et al. Macroscopic domain formation during cooling in the platelet plasma membrane: An issue of low cholesterol content. en. Biochimica et Biophysica Acta (BBA) - Biomembranes 1788, 1229-1237. issn: 00052736. https://linkinghub.elsevier.com/retrieve/pii/S000527360900100X (2023) (jun. de 2009).33. Doktorova, M. et al. Cell membranes sustain phospholipid imbalance via cholesterol asymmetry. bioRxiv, 2023-07 (2023).34. Alleva, K. y Federico, L. Análisis estructuralista de las teorías de Hill: una elucidación de explicación en bioquímica. Scientiae Studia 11, 333-353 (2013)35. Grau-Campistany, A., Manresa, A., Pujol, M., Rabanal, F. y Cajal, Y. Tryptophancontaining lipopeptide antibiotics derived from polymyxin B with activity against Gram positive and Gram negative bacteria. Biochimica et Biophysica Acta (BBA)-Biomembranes 1858, 333-343 (2016).36. Koller, D. y Lohner, K. The role of spontaneous lipid curvature in the interaction of interfacially active peptides with membranes. Biochimica et Biophysica Acta (BBA)-Biomembranes 1838, 2250-2259 (2014).37. Heerklotz, H., Wieprecht, T. y Seelig, J. Membrane perturbation by the lipopeptide surfactin and detergents as studied by deuterium NMR. 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