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dc.contributor.authorOrtiz López, Claudia-
dc.date.accessioned2021-12-09T23:47:28Z-
dc.date.available2021-12-09T23:47:28Z-
dc.date.issued2019-12-20-
dc.identifier.urihttps://repositorio.accefyn.org.co/handle/001/1167-
dc.description.abstractLos péptidos antimicrobianos han atraído mucha atención como nuevos agentes terapéuticos contra enfermedades infecciosas. En este estudio se hizo el diseño racional in silico de 18 péptidos catiónicos con actividad antimicrobiana contra bacterias patógenas resistentes utilizando el programa DEPRAMP desarrollado en el Grupo de Investigación en Bioquímica y Microbiología de la Universidad Industrial de Santander. Posteriormente, los péptidos diseñados se sintetizaron en fase sólida con el método de 9-fluorenilmetoxicarbonilo en medio ácido. Se obtuvieron secuencias cortas de 17 aminoácidos con un grado de pureza entre 95 y 98 %, estructura secundaria de hélice alfa, carga neta catiónica (entre +3 y +6), punto isoeléctrico entre 10,04 y 12,03 e índice de hidropatía entre -0,62 y 1,14. Todos los péptidos antimicrobianos mostraron actividad antibacteriana y bactericida in vitro frente al menos una de las cepas patógenas estudiadas: Escherichia coli O157: H7, Pseudomonas aeruginosa y Staphylococcus aureus resistente a la meticilina. Los péptidos antimicrobianos GIBIM-P5S9K y GIBIM-P5F8W registraron la mejor actividad antibacteriana, alcanzando una concentración mínima inhibitoria (CMI 99) en rangos de 0,5 a 25 μM frente a las tres cepas evaluadas, de las cuales Escherichia coli O157: H7 fue la más sensible frente al péptido antimicrobiano GIBIMP5F8W, con una CMI 99 de 0,5 μM y una concentración mínima bactericida de 10 μM, en tanto que la cepa de Pseudomonas aeruginosa fue la más resistente, con una CMI de más de 100 μM frente a más de cinco péptidos antimicrobianos. La toxicidad de los péptidos sobre los eritrocitos produjo un porcentaje de hemólisis menor al 40 % en concentraciones de 50 μM. Por su parte, en las líneas celulares de carcinoma de pulmón A549 y HepG2, el único compuesto que presentó toxicidad fue GIBIM-P5F8W, presentando un 36% de células viables en concentraciones de 100 μM del péptido en la línea celular A549.spa
dc.description.abstractAntimicrobial peptides have attracted much attention as new therapeutic agents against infectious diseases. In this work, we made the rational in silico design of 18 cationic peptides with antimicrobial activity against resistant pathogenic bacteria using the DEPRAMP software developed in the GIBIM research group. Subsequently, the designed peptides were synthesized in solid phase using the Fmoc strategy in an acid medium. Then, sequences of 17 amino acids were obtained with a degree of purity between 95 and 98%, secondary structure α-helix, net cationic charge (between +3 and +6), pI between 10.04 to 12.03, and hydropathy index between -0.62 and 1.14. All antimicrobial peptides showed antibacterial and bactericidal activity in vitro against at least one of the pathogenic strains studied: Escherichia coli O157: H7, Pseudomonas aeruginosa, and Staphylococcus aureus Resistant to Methicillin. The GIBIM-P5S9K and GIBIM-P5F8W antimicrobial peptides presented the best antibacterial activities reaching MIC99 in ranges of 0.5 to 25 μM against the three strains evaluated. E. coli O157: H7 was the most sensitive strain to the GIBIMP5F8W presenting 0.5 μM MIC99 and 10 μM MBC, and P. aeruginosa was the most resistant strain with MIC values over 100 μM against more than five antimicrobial peptides. The toxicity of peptides in erythrocytes produced a hemolysis percentage of less than 40% in concentrations of 50 μM. On the other hand, in the lung carcinoma cell lines A549 and HepG2, the only compound that presented toxicity was GIBIM-P5F8W, presenting 36% of viable cells in concentrations of 100 μM of the peptide in the A549 cell line.eng
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dc.publisherAcademia Colombiana de Ciencias Exactas, Físicas y Naturalesspa
dc.rightsCreative Commons Attribution-NonCommercial-ShareAlike 4.0 Internationalspa
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/spa
dc.sourceRevista de la Academia Colombiana de Ciencias Exactas, Físicas y Naturalesspa
dc.titleDiseño, síntesis, caracterización y evaluación in vitro de la actividad de los péptidos antimicrobianos contra bacterias patógenas resistentes a antibióticosspa
dc.typeArtículo de revistaspa
dcterms.audienceEstudiantes, Profesores, Comunidad científica colombianaspa
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dc.rights.creativecommonsAtribución-NoComercial 4.0 Internacional (CC BY-NC 4.0)spa
dc.identifier.doihttps://doi.org/10.18257/raccefyn.864-
dc.subject.proposalPéptidos antimicrobianosspa
dc.subject.proposalAntimicrobial peptideseng
dc.subject.proposalResistencia microbianaspa
dc.subject.proposalMicrobial resistanceeng
dc.subject.proposalactividad antimicrobianaspa
dc.subject.proposalAntimicrobial activityeng
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dc.relation.ispartofjournalRevista de la Academia Colombiana de Ciencias Exactas, Físicas y Naturalesspa
dc.relation.citationvolume43spa
dc.relation.citationstartpage614spa
dc.relation.citationendpage627spa
dc.publisher.placeBogotá, Colombiaspa
dc.contributor.corporatenameAcademia Colombiana de Ciencias Exactas, Físicas y Naturalesspa
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