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Isolating and characterizing antimicrobial peptides derived from larvae of the blowfly Sarconesiopsis magellanica (diptera: Calliphoridae)

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dc.contributor.advisorBello García, Felio Jesús
dc.contributor.advisorPatarroyo, Manuel A.
dc.creatorDíaz Roa, Andrea
dc.creator.degreeDoctor en Ciencias Biomédicas y Biológicasspa
dc.creator.degreetypeFull timespa
dc.date.accessioned2019-10-18T16:50:35Z
dc.date.available2019-10-18T16:50:35Z
dc.date.created2019-08-28
dc.description.abstractLarval therapy (LT) is an alternative treatment which uses fly larvae to heal chronic wounds; its action is based on debridement, bacterial removal and stimulating granulation tissue. The most important mechanism for fighting infection with LT depends on larval excretions and secretions (ES). The larvae are protected by an antimicrobial peptide (1) spectrum. Sarconesiopsis magellanica is a promising necrophagous fly for use in medicine. This study was thus aimed at identifying and characterizing S. magellanica AMPs contained in ES, for the first time. ES were fractionated by RP-HPLC using C18 columns. The products were lyophilized, and their antimicrobial activity characterized. The sequences were determined by mass spectrometry. The mechanism of action was evaluated by fluorescence and electronic microscopy. Toxicity was tested on HeLA cells and human erythrocytes; the physicochemical properties of the identified peptides were evaluated. Two molecules in the ES were characterized: sarconesin (a new peptide having antibacterial activity against Gram-negative (Escherichia coli D31, Pseudomonas aeruginosa 27853) and Gram-positive (Staphylococcus aureus ATCC 29213, Micrococcus luteus A270) bacteria and sarconsesin II, having activity against Gram-negative (E. coli MG1655, P. aeruginosa ATCC 27853) and Gram-positive (S. aureus ATCC 29213, M. luteus A270) bacteria. The minimum inhibitory concentrations ranged from 1.2 μM upwards; the AMPs did not have toxicity in any tested cells and their action on bacterial membrane and DNA was confirmed. Sarconesin had similarity with the CDC42 protein belonging to the Rho-family of GTPases which are important in organelle development and wound repair. Sarconesin II was seen to be a conserved domain of the ATP synthase protein belonging to the FliI superfamily. The data reported here indicates that the peptides could be alternative therapeutic candidates for use in infections against Gram-negative and Gram-positive microorganisms and as new resources to combat resistance against antimicrobial agents.eng
dc.description.sponsorshipColcienciasspa
dc.description.sponsorshipButantan Institutespa
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.48713/10336_20460
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/20460
dc.language.isoengspa
dc.publisherUniversidad del Rosariospa
dc.publisher.departmentFacultad de Ciencias Naturales y Matemáticasspa
dc.publisher.programDoctorado en Ciencias Biomédicas y Biológicasspa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.rights.licenciaPARGRAFO: En caso de presentarse cualquier reclamación o acción por parte de un tercero en cuanto a los derechos de autor sobre la obra en cuestión, EL AUTOR, asumirá toda la responsabilidad, y saldrá en defensa de los derechos aquí autorizados; para todos los efectos la universidad actúa como un tercero de buena fe.
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dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subjectAntimicrobial peptidespa
dc.subjectLarval therapyspa
dc.subjectSarconesiopsis magellanicaspa
dc.subject.ddcCiencias médicas, Medicinaspa
dc.subject.lembMedicinaspa
dc.subject.lembPeptidosspa
dc.titleIsolating and characterizing antimicrobial peptides derived from larvae of the blowfly Sarconesiopsis magellanica (diptera: Calliphoridae)spa
dc.typedoctoralThesiseng
dc.type.documentTesisspa
dc.type.hasVersioninfo:eu-repo/semantics/acceptedVersion
dc.type.spaTesis de doctoradospa
local.department.reportEscuela de Medicina y Ciencias de la Saludspa
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Doctorado en Ciencias Biomédicas y Biológicas