Effect of the amphipatic a-helix structure and the cysteine redox state of gibim-p5 analogues on the antimicrobial activity against escherichia coli o157:h7, methicillin resistant staphylococcus aureus and pseudomonas aeruginosa

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dc.contributor.advisorUrquiza Martinez, Mauricio
dc.contributor.advisorMéndez Sánchez, Stelia Carolina
dc.contributor.authorBautista Garces, Yenny Paola
dc.date.accessioned2024-03-04T00:13:55Z
dc.date.available2018
dc.date.available2024-03-04T00:13:55Z
dc.date.created2018
dc.date.issued2018
dc.description.abstractEl efecto de la estructura secundaria -hélice y el estado redox de la cisteína sobre la actividad antimicrobiana de GIBIM-P5 se estudió mediante el diseño de siete péptidos análogos. La secuencia GIBIM-P5 se modificó para aumentar o disminuir la estabilidad de la -hélice cambiando los residuos Gly por Ala o por residuos Pro, respectivamente. Además, los residuos de Phe y Cys fueron cambiados por Trp y Ser, respectivamente; en algunos péptidos análogos, se incluyó una Cys adicional cambiando uno de los residuos de la secuencia peptídica. Cuando los residuos de Gly fueron cambiados por Ala para generar GAM019, la MIC99 disminuyó de 10 a 1Escherichia coli 0157: H7 (E. coli O157: H7); por el contrario, cuando los residuos de Gly fueron cambiados por Pro en GAM020, la MIC99 (33,7%), seguido de GIBIM-P5 (22,5%) y menor para GAM020 (2,9%). La actividad antibacteriana de péptidos análogos con dos Cys fue mayor cuando ambos estaban en el mismo lado de la -hélice, (GAM022 y GAM023) que cuando estos Cys estaban en el lado opuesto (GAM024 y GAM025). Curiosamente, estos péptidos presentaron baja citotoxicidad frente a las células de mamíferos, presentando un índice terapéutico entre 2 y 88, que eran más altos que el índice de GIBIM-P5, mostraron un alto potencial para ser utilizados contra P. aeruginosa y SARM.
dc.description.abstractenglishThe effect of the secondary -helix structure and the cysteine redox state on the antimicrobial activity of GIBIM-P5 was studied by design seven analogue peptides. GIBIM-P5 sequence was modified to increase or decrease the -helix stability by changing Gly residues by Ala or by Pro residues, respectively. Moreover, the Phe and Cys residues were changed by Trp and Ser, respectively; in some analogue peptides an additional Cys was included by changing one of the peptide sequence residue. When the Gly residues were changed by Ala to generate GAM019 the MIC99 decreased from 10 to 1.48 µM for Pseudomonas aeruginosa (P. aeruginosa), from 100 to 4.32 µM for Methicillin-resistant Staphylococcus aureus (SARM) and from 100 to 29.34 µM for Escherichia coli 0157:H7 (E.coli O157:H7); on the contrary, when Gly residues were changed by Pro in GAM020 the MIC99 increased to 29 µM for P. aeruginosa, to 91 µM for SARM and to 132 µM for E. coli O157:H7. The helical content was higher for GAM019 (33.7%), followed by GIBIM-P5 (22.5%) and lower for GAM020 (2.9%). The antibacterial activity of analogue peptides having two Cys was higher when both of them were on the same side of the -helix, (GAM022 and GAM023) than when these Cys were on the opposite side, (GAM024 and GAM025). Interestingly, these peptides presented low cytotoxity against mammalian cells, displaying and therapeutic index between 2 and 88, which were higher than the index of GIBIM-P5, having showed high potential to be used against P. aeruginosa and SARM.Research project to
dc.description.degreelevelPregrado
dc.description.degreenameQuímico
dc.format.mimetypeapplication/pdf
dc.identifier.instnameUniversidad Industrial de Santander
dc.identifier.reponameUniversidad Industrial de Santander
dc.identifier.repourlhttps://noesis.uis.edu.co
dc.identifier.urihttps://noesis.uis.edu.co/handle/20.500.14071/39396
dc.language.isospa
dc.publisherUniversidad Industrial de Santander
dc.publisher.facultyFacultad de Ciencias
dc.publisher.programQuímica
dc.publisher.schoolEscuela de Química
dc.rightshttp://creativecommons.org/licenses/by/4.0/
dc.rights.accessrightsinfo:eu-repo/semantics/openAccess
dc.rights.creativecommonsAtribución-NoComercial-SinDerivadas 4.0 Internacional (CC BY-NC-ND 4.0)
dc.rights.licenseAttribution-NonCommercial 4.0 International (CC BY-NC 4.0)
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0
dc.subjectPeptidos Antmicrobianos/ Estructura -Hélice/ P.Aeruginosa/ Sarm/ E.Coli O157:H7
dc.subject.keyword-Helix Structure / P.Aeruginosa / Sarm / E.Coli O157:H7
dc.titleEffect of the amphipatic a-helix structure and the cysteine redox state of gibim-p5 analogues on the antimicrobial activity against escherichia coli o157:h7, methicillin resistant staphylococcus aureus and pseudomonas aeruginosa
dc.title.english-helix structure and the cysteine redox state of gibim-p5 analogues on the antimicrobial activity against escherichia coli o157:h7, methicillin resistant staphylococcus aureus and pseudomonas aeruginosa*
dc.type.coarhttp://purl.org/coar/version/c_b1a7d7d4d402bcce
dc.type.hasversionhttp://purl.org/coar/resource_type/c_7a1f
dc.type.localTesis/Trabajo de grado - Monografía - Pregrado
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