Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos

Detalhes bibliográficos
Autor(a) principal: Ferreira, Carolina Silva
Data de Publicação: 2018
Tipo de documento: Dissertação
Idioma: por
Título da fonte: Repositório Institucional da UFVJM
Texto Completo: http://acervo.ufvjm.edu.br/jspui/handle/1/1995
Resumo: ?rea de concentra??o: Qu?mica Org?nica.
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spelling Ferreira, Carolina SilvaVerly, Rodrigo MoreiraOliveira, Patricia Machado dePinheiro, Anderson de S?Martins, Helen RodriguesMagalh?es, Mariana Torquato Quezado deUniversidade Federal dos Vales do Jequitinhonha e Mucuri (UFVJM)Verly, Rodrigo Moreira2019-07-02T18:53:59Z2019-07-02T18:53:59Z20182018-12-14FERREIRA, Carolina Silva. Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos. 2018. 108 p. Disserta??o (Mestrado) ? Programa de P?s-Gradua??o em Qu?mica, Universidade Federal dos Vales do Jequitinhonha e Mucuri, Diamantina, 2018.http://acervo.ufvjm.edu.br/jspui/handle/1/1995?rea de concentra??o: Qu?mica Org?nica.Os pept?deos bioativos, devido ao amplo espectro de atividade, tem resultado em um aumento significativo nos estudos dessas mol?culas, como alternativas estrat?gicas para enfrentar problemas como a resist?ncia aos antibi?ticos convencionais. O mecanismo de a??o de pept?deos antimicrobianos em grande parte ocorre pela intera??o com a membrana do microrganismo, causando uma perturba??o da organiza??o da bicamada lip?dica, podendo ocasionar a lise celular. Entretanto, os detalhes desta intera??o ainda n?o s?o totalmente conhecidos e, portanto, estudos da intera??o pept?deo-membrana com meios biomim?ticos fazem-se necess?rios. O presente trabalho descreve a s?ntese e caracteriza??o dos pept?deos antimicrobianos, D-fenilseptina (D-Phes), L-fenilseptina (L-Phes) e um potencial pept?deo bioativo desenhado a partir da sequ?ncia prim?ria da prote?na SmKI-1, denominado de pept?deo Schistocina-2, para estudos da intera??o pept?deo-membrana. Assim, foram empregadas como ferramentas principais de investiga??o a Calorimetria de Titula??o Isot?rmica (ITC), a Resson?ncia Magn?tica Nuclear (RMN), a Espectroscopia de Dicro?smo Circular (CD), o espalhamento de luz din?mico (DLS) e medidas de Potencial Zeta. Todos os experimentos foram desenvolvidos em meios que mimetizam os ambientes de membranas, tais como micelas e ves?culas fosfolip?dicas. Para as fenilseptinas, foi observado que a diferen?a estereoqu?mica do segundo res?duo de fenilalanina (F-2) da regi?o N-terminal altera a atividade frente a bact?rias, sendo a D-Phes mais ativa contra as bact?rias testadas. Segundo estudo por RMN, foi identificado que D-Phes possui um maior momento hidrof?bico, sugerindo que, por isso, poderia se inserir mais na superf?cie da membrana e interagir de maneira mais efetiva do que L-Phes. Esse dado p?de ser confirmado por estudos de ITC, DLS e Potencial Zeta que mostraram tamb?m a maior intera??o de DPhes em rela??o ao seu ep?mero. Al?m disso, foi comprovado que este pept?deo tamb?m possui maior atividade antif?ngica e tamb?m citot?xica, quando testado em c?lulas metast?ticas de c?ncer de mama, com rela??o a L-Phes. A segunda parte deste trabalho apresenta os estudos realizados com um novo pept?deo, Schistocina-2, desenhado a partir de uma prote?na, com o objetivo de obter um novo agente antimicrobiano. As an?lises de CD e RMN mostraram que esse pept?deo se estrutura em ?-h?lice quando em contato com meios mim?ticos de membrana. Al?m disso, estudos de ITC, DLS e Potencial Zeta mostraram que a intera??o de Schistocina-2 ? efetiva, perturbando a membrana fosfolip?dica e alterando a carga superficial da mesma. Portanto, ? apresentado um pept?deo in?dito com potencial biotecnol?gico.Submitted by Nivaldo Melo (nivaldo.melo@ufvjm.edu.br) on 2019-07-01T16:54:14Z No. of bitstreams: 2 license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5) carolina_silva_ferreira.pdf: 5174721 bytes, checksum: 7104b1e92a0d61b35415ba456de06438 (MD5)Approved for entry into archive by Jos? Henrique Henrique (jose.neves@ufvjm.edu.br) on 2019-07-02T18:53:59Z (GMT) No. of bitstreams: 2 license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5) carolina_silva_ferreira.pdf: 5174721 bytes, checksum: 7104b1e92a0d61b35415ba456de06438 (MD5)Made available in DSpace on 2019-07-02T18:53:59Z (GMT). No. of bitstreams: 2 license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5) carolina_silva_ferreira.pdf: 5174721 bytes, checksum: 7104b1e92a0d61b35415ba456de06438 (MD5) Previous issue date: 2018Disserta??o (Mestrado) ? Programa de P?s-Gradua??o em Qu?mica, Universidade Federal dos Vales do Jequitinhonha e Mucuri, 2018.Bioactive peptides, due to the broad spectrum of activity, have resulted in a significant increase in the studies of these molecules as strategic alternatives to tackle problems such as resistance to conventional antibiotics. The mechanism of action of antimicrobial peptides largely occurs through interaction with the membrane of the microorganism, causing a disturbance of the organization of the lipid bilayer, which can lead to cell lysis. However, the details of this interaction are not yet fully understood and, therefore, membrane-peptide interaction studies with biomimetic media are necessary. The present work describes the synthesis and characterization of antimicrobial peptides, Dphenylseptin (D-Phes), L-phenylseptin (L-Phes) and a potential bioactive peptide designed from the primary sequence of the SmKI-1 protein, known as the Schistocine-2 peptide, for studies of membrane-peptide interaction. Thus, we used as main research tools Isothermal Titration Calorimetry (ITC), Nuclear Magnetic Resonance (NMR), Circular Dichroism Spectroscopy (CD), Dynamic Light Scattering (DLS) and Zeta Potential Measurements. All experiments were developed in media that mimic membrane environments, such as micelles and phospholipid vesicles. For the phenylseptin, it was observed that the stereochemical difference of the second phenylalanine residue (F-2) of the N-terminal region changes the activity against bacteria, being D-Phes more active against the bacteria tested. According to the study by NMR, it was identified that D-Phes has a higher hydrophobic moment, suggesting that, therefore, it could be inserted more on the surface of the membrane and interact more effectively than L-Phes. This data could be confirmed by studies of ITC, DLS and Potential Zeta that also showed the greater interaction of D-Phes with respect to its epimer. In addition, it has been proven that this peptide also has higher antifungal and also cytotoxic activity, when tested in metastatic breast cancer cells, in relation to LPhes. The second part of this work presents the studies carried out with a new peptide, Schistocin-2, designed from a protein, with the aim of obtaining a new antimicrobial agent. CD and NMR analyzes showed that this peptide is ?-helix-structured when in contact with membrane mimetic media. In addition, studies of ITC, DLS and Potential Zeta showed that the interaction of Schistocin-2 is effective, disturbing the phospholipid membrane and altering the surface charge of the same. Therefore, an unpublished peptide with biotechnological potential is presented.porUFVJMA concess?o da licen?a deste item refere-se ao ? termo de autoriza??o impresso assinado pelo autor, assim como na licen?a Creative Commons, com as seguintes condi??es: Na qualidade de titular dos direitos de autor da publica??o, autorizo a Universidade Federal dos Vales do Jequitinhonha e Mucuri e o IBICT a disponibilizar por meio de seus reposit?rios, sem ressarcimento dos direitos autorais, de acordo com a Lei n? 9610/98, o texto integral da obra disponibilizada, conforme permiss?es assinaladas, para fins de leitura, impress?o e/ou download, a t?tulo de divulga??o da produ??o cient?fica brasileira, e preserva??o, a partir desta data.info:eu-repo/semantics/openAccessEstudos do modo de intera??o de pept?deos bioativos com meios biomim?ticosStudies of the mode of interaction of bioative peptide with biomimetic mediainfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisPept?deosAntimicrobianosIntera??oMembranaFenilseptinaSchistocina-2SmKI-1PeptidesAntimicrobialInteractionMembranePhenylseptinSchistocin-2reponame:Repositório Institucional da UFVJMinstname:Universidade Federal dos Vales do Jequitinhonha e Mucuri (UFVJM)instacron:UFVJMTEXTcarolina_silva_ferreira.pdf.txtcarolina_silva_ferreira.pdf.txtExtracted texttext/plain184877http://acervo.ufvjm.edu.br/jspui/bitstream/1/1995/6/carolina_silva_ferreira.pdf.txt971f789cb1b058cef42fc37982f3bfb5MD56LICENSElicense.txtlicense.txttext/plain; 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dc.title.pt_BR.fl_str_mv Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos
dc.title.alternative.en.fl_str_mv Studies of the mode of interaction of bioative peptide with biomimetic media
title Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos
spellingShingle Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos
Ferreira, Carolina Silva
Pept?deos
Antimicrobianos
Intera??o
Membrana
Fenilseptina
Schistocina-2
SmKI-1
Peptides
Antimicrobial
Interaction
Membrane
Phenylseptin
Schistocin-2
title_short Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos
title_full Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos
title_fullStr Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos
title_full_unstemmed Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos
title_sort Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos
author Ferreira, Carolina Silva
author_facet Ferreira, Carolina Silva
author_role author
dc.contributor.references.none.fl_str_mv Verly, Rodrigo Moreira
Oliveira, Patricia Machado de
Pinheiro, Anderson de S?
Martins, Helen Rodrigues
dc.contributor.advisorco.none.fl_str_mv Magalh?es, Mariana Torquato Quezado de
dc.contributor.institution.pt_BR.fl_str_mv Universidade Federal dos Vales do Jequitinhonha e Mucuri (UFVJM)
dc.contributor.author.fl_str_mv Ferreira, Carolina Silva
dc.contributor.advisor1.fl_str_mv Verly, Rodrigo Moreira
contributor_str_mv Verly, Rodrigo Moreira
dc.subject.keyword.pt_BR.fl_str_mv Pept?deos
Antimicrobianos
Intera??o
Membrana
Fenilseptina
Schistocina-2
SmKI-1
topic Pept?deos
Antimicrobianos
Intera??o
Membrana
Fenilseptina
Schistocina-2
SmKI-1
Peptides
Antimicrobial
Interaction
Membrane
Phenylseptin
Schistocin-2
dc.subject.keyword.en.fl_str_mv Peptides
Antimicrobial
Interaction
Membrane
Phenylseptin
Schistocin-2
description ?rea de concentra??o: Qu?mica Org?nica.
publishDate 2018
dc.date.submitted.none.fl_str_mv 2018-12-14
dc.date.issued.fl_str_mv 2018
dc.date.accessioned.fl_str_mv 2019-07-02T18:53:59Z
dc.date.available.fl_str_mv 2019-07-02T18:53:59Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/masterThesis
format masterThesis
status_str publishedVersion
dc.identifier.citation.fl_str_mv FERREIRA, Carolina Silva. Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos. 2018. 108 p. Disserta??o (Mestrado) ? Programa de P?s-Gradua??o em Qu?mica, Universidade Federal dos Vales do Jequitinhonha e Mucuri, Diamantina, 2018.
dc.identifier.uri.fl_str_mv http://acervo.ufvjm.edu.br/jspui/handle/1/1995
identifier_str_mv FERREIRA, Carolina Silva. Estudos do modo de intera??o de pept?deos bioativos com meios biomim?ticos. 2018. 108 p. Disserta??o (Mestrado) ? Programa de P?s-Gradua??o em Qu?mica, Universidade Federal dos Vales do Jequitinhonha e Mucuri, Diamantina, 2018.
url http://acervo.ufvjm.edu.br/jspui/handle/1/1995
dc.language.iso.fl_str_mv por
language por
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv UFVJM
publisher.none.fl_str_mv UFVJM
dc.source.none.fl_str_mv reponame:Repositório Institucional da UFVJM
instname:Universidade Federal dos Vales do Jequitinhonha e Mucuri (UFVJM)
instacron:UFVJM
instname_str Universidade Federal dos Vales do Jequitinhonha e Mucuri (UFVJM)
instacron_str UFVJM
institution UFVJM
reponame_str Repositório Institucional da UFVJM
collection Repositório Institucional da UFVJM
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