Diseño de un péptido con actividad antibiótica selectiva derivado de la Miotoxina II presente en el veneno de la serpiente Bothrops Asper mediante diseño racional in silico y evaluación de su capacidad antibiótica

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dc.contributor.advisorGuevara Pulido, James Oswaldo
dc.contributor.authorHuertas Gómez, Laura Tatiana
dc.date.accessioned2024-11-20T02:50:25Z
dc.date.available2024-11-20T02:50:25Z
dc.date.issued2024-11
dc.description.abstractLa resistencia bacteriana es una preocupación de salud pública, especialmente ante patógenos reportados como prioritarios por la OMS, como Escherichia coli resistente a carbapenémicos [1]. Como alternativa a los antibióticos actuales, las toxinas animales han suscitado un notable interés. Este trabajo realiza el diseño racional de un péptido antibiótico derivado de la secuencia 115-129 de la Miotoxina II, presente en el veneno de la serpiente Bothrops asper [2]. Se realizaron 20 modificaciones a la secuencia original 115-129 mediante docking molecular, identificando al péptido KHWYKHYRH como el de mejor energía de afinidad (-7.6 kcal/mol) hacia el lipopolisacárido (LPS). El perfil de toxicidad del péptido análogo realizado mediante ADMETlab 3.0 sugirió bajas probabilidades de cardiotoxicidad (0.047), mutagenicidad (0.136) y carcinogenicidad (0.0). Finalmente, los ensayos de difusión en agar no mostraron actividad antibacteriana significativa. No obstante, se sugiere que la protonación del péptido podría potenciar su efectividad. Adicionalmente, el desarrollo de un sistema de liberación del péptido podría optimizar su permeabilidad a través de la membrana bacteriana.
dc.description.abstractenglishBacterial resistance is a public health concern, especially against pathogens reported as priority by the WHO, such as carbapenem-resistant Escherichia coli [1]. As an alternative to current antibiotics, animal toxins have aroused considerable interest. This work performs the rational design of an antibiotic peptide derived from the sequence 115-129 of Myotoxin II, present in the venom of the snake Bothrops asper [2]. Twenty modifications were made to the original sequence 115-129 by molecular docking, identifying the peptide KHWYKHYRH as the one with the best affinity energy (-7.6 kcal/mol) towards lipopolysaccharide (LPS). The toxicity profile of the analogous peptide performed using ADMETlab 3.0 suggested low probabilities of cardiotoxicity (0.047), mutagenicity (0.136) and carcinogenicity (0.0). Finally, agar diffusion assays did not show significant antibacterial activity. However, it is suggested that protonation of the peptide could enhance its effectiveness. Additionally, the development of a peptide delivery system could optimize its permeability through the bacterial membrane.
dc.description.degreelevelPregradospa
dc.description.degreelevelQuímico Farmacéuticospa
dc.format.mimetypeapplication/pdf
dc.identifier.instnameUniversidad El Bosquespa
dc.identifier.reponamereponame:Repositorio Institucional Universidad El Bosquespa
dc.identifier.repourlrepourl:https://repositorio.unbosque.edu.co
dc.identifier.urihttps://hdl.handle.net/20.500.12495/13262
dc.language.isoes
dc.publisher.facultyFacultad de Cienciasspa
dc.publisher.grantorUniversidad El Bosquespa
dc.publisher.programQuímica Farmacéuticaspa
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dc.rightsAtribución-NoComercial-CompartirIgual 4.0 Internacionalen
dc.rights.accessrightsinfo:eu-repo/semantics/openAccess
dc.rights.accessrightshttp:/purl.org/coar/access_right/c_abf2/
dc.rights.localAcceso abiertospa
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.subjectResistencia bacteriana
dc.subjectEscherichia coli
dc.subjectMiotoxina II
dc.subjectAntibiótico
dc.subjectDocking molecular
dc.subjectLipopolisacárido
dc.subject.ddc615.19
dc.subject.keywordsBacterial resistance
dc.subject.keywordsEscherichia coli
dc.subject.keywordsMyotoxin II
dc.subject.keywordsAntibiotic
dc.subject.keywordsMolecular docking
dc.subject.keywordsLipopolysaccharide
dc.titleDiseño de un péptido con actividad antibiótica selectiva derivado de la Miotoxina II presente en el veneno de la serpiente Bothrops Asper mediante diseño racional in silico y evaluación de su capacidad antibiótica
dc.title.translatedDesign of a peptide with selective antibiotic activity derived from Myotoxin II present in the venom of the snake Bothrops Asper through rational in silico design and evaluation of its antibiotic capacity
dc.type.coarhttps://purl.org/coar/resource_type/c_7a1f
dc.type.coarversionhttps://purl.org/coar/version/c_ab4af688f83e57aa
dc.type.driverinfo:eu-repo/semantics/bachelorThesis
dc.type.hasversioninfo:eu-repo/semantics/acceptedVersion
dc.type.localTesis/Trabajo de grado - Monografía - Pregrado

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