Design and synthesis of self-assembling peptides with binding affinity to hyaluronan
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Tipo de documento: | Dissertação |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.14/37036 |
Resumo: | Hyaluronan (HA) is a natural polymer that due to its viscoelasticity, good biocompatibility and a conformational flexibility, has been a polysaccharide of great interest to the scientists that is used in various biomedical and clinical applications such as tissue engineering, biomaterials engineering and cosmetics. This project aimed to explore the self-assembly between hyaluronan (HA) and HA-binding peptides derived from Pep-1[NH2-GAHWQFNALTVR-NH2], a peptide known to bind HA and identified by phage display. Six variations of Pep-1 were synthesized to test if they can form new nanostructures with HA. Peptides with alkyl chains allow the formation of highly stable self-assembled nanostructures. Considering this fact, were synthesized four peptides with these properties in order to try the interaction between them and hyaluronan. On the other hand, thiols (compounds that contain a SH group) can bond to gold due to the capability to be chemisorbed on metal surfaces, forming a very stable metal-sulfur bonds. Therefore, it was synthesized a peptide with a tail constituted by Mercaptoethanol acid that is expected to react with gold, displaying the Pep-1 free to interact with HA. Electrospray Ionization Mass Spectrometry and High-Performance Liquid Chromatography techniques were used to characterize and purify the peptides, respectively. After the experimental work and its results, it was concluded that by increasing the percentage of Pep-1 is possible to see an interaction between it and hyaluronan. Peptides with longer alkyl chain are to hydrophobic to be purified and consequently it was impossible to study the interaction between them and HA.When the alkyl chains become shorter, the peptides become less hydrophobic and their purification is possible. Though, the peptides with shorter chains can´t allow the formation of self-assembled structures. The peptide that has a Mercaptoethanol acid is hydrophobic but, its purification is possible. More tests should be done in order to study and analyze if the interaction between this last peptide and HA is possible. |
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Design and synthesis of self-assembling peptides with binding affinity to hyaluronanDomínio/Área Científica::Ciências Médicas::Biotecnologia MédicaHyaluronan (HA) is a natural polymer that due to its viscoelasticity, good biocompatibility and a conformational flexibility, has been a polysaccharide of great interest to the scientists that is used in various biomedical and clinical applications such as tissue engineering, biomaterials engineering and cosmetics. This project aimed to explore the self-assembly between hyaluronan (HA) and HA-binding peptides derived from Pep-1[NH2-GAHWQFNALTVR-NH2], a peptide known to bind HA and identified by phage display. Six variations of Pep-1 were synthesized to test if they can form new nanostructures with HA. Peptides with alkyl chains allow the formation of highly stable self-assembled nanostructures. Considering this fact, were synthesized four peptides with these properties in order to try the interaction between them and hyaluronan. On the other hand, thiols (compounds that contain a SH group) can bond to gold due to the capability to be chemisorbed on metal surfaces, forming a very stable metal-sulfur bonds. Therefore, it was synthesized a peptide with a tail constituted by Mercaptoethanol acid that is expected to react with gold, displaying the Pep-1 free to interact with HA. Electrospray Ionization Mass Spectrometry and High-Performance Liquid Chromatography techniques were used to characterize and purify the peptides, respectively. After the experimental work and its results, it was concluded that by increasing the percentage of Pep-1 is possible to see an interaction between it and hyaluronan. Peptides with longer alkyl chain are to hydrophobic to be purified and consequently it was impossible to study the interaction between them and HA.When the alkyl chains become shorter, the peptides become less hydrophobic and their purification is possible. Though, the peptides with shorter chains can´t allow the formation of self-assembled structures. The peptide that has a Mercaptoethanol acid is hydrophobic but, its purification is possible. More tests should be done in order to study and analyze if the interaction between this last peptide and HA is possible.O ácido hialurónico é um polímero natural que, devido á sua viscoelasticidade, boa biocompatibilidade e conformação flexível, nos últimos anos tem sido alvo de grande interesse por parte da comunidade científica sendo utilizado em inúmeras aplicações clínicas e biomédicas tais como engenharia de tecidos , engenharia de biomateriais e cosmética. Este projecto teve como objectivo explorar processos de organização molecular para desenvolver biomateriais combinando o ácido hialurónico, com péptidos com afininidade para este polímero, como o péptido identificado por “phage display” (Pep-1, [NH2-GAHWQFNALTVR-NH2]). Para tal, foram sintetizadas seis variações do Pep-1 com o objectivo de testar se estas formam nanoestruturas em conjunto com o ácido hialurónico. Os péptidos com cadeias alquilo permitem a auto-organização para formação de nanoestruturas altamente estáveis. Considerando este facto, foram sintetizados quatro péptidos com estas propriedades para tentar a interação entre eles e o ácido hialurónico. Por outro lado, os tióis (compostos que contêm um grupo SH) podem ligar-se ao ouro devido à sua capacidade de adsorção química em superfícies metálicas, formando uma ligação metal-enxofre muito estável. Foi, portanto, sintetizado um péptido com uma terminação constituída por ácido mercaptoetanol de forma a que este reagisse com o ouro deixando o Pep-1 livre para interagir com ácido hialurónico. Foram usadas as técnicas de Espectrometria de Massa com Ionização Electrospray e and Cromatografia líquida de alta eficiência para caracterizar e purificar os péptidos. Após o trabalho experimental e respectivos resultados, foi concluído que aumentando a percentagem do péptido Pep-1, é possível ver uma interacção entre este e o ácido hialurónico. Os péptidos com cadeia alquilo mais longa são muito hidrofóbicos para serem purificados e consequentemente é impossível estudar a interacção entre estes e o ácido hialurónico. Quando as cadeias alquilo se tornam mais curtas, os péptidos tornam-se menos hidrofóbicos e a sua purificação é possível. No entanto, os peptídeos com cadeias mais curtas não permitem a formação de estruturas construídas por processos de auto-organização molecular. O péptido que possui uma terminação constituída pelo ácido mercaptoetanol é hidrofóbico, mas, embora difícil, a sua purificação é possível. Mais testes devem ser realizados com o objectivo de analisar e caracterizar se a interacção entre este último péptido e o ácido hialurónico é possível.Azevedo, HelenaCollis, DominicVeritati - Repositório Institucional da Universidade Católica PortuguesaDória, Rita Saraiva de Aragão da Silva2022-03-15T16:19:29Z2017-07-062017-012017-07-06T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttp://hdl.handle.net/10400.14/37036TID:202729842enginfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-12T17:42:28Zoai:repositorio.ucp.pt:10400.14/37036Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:30:06.664016Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Design and synthesis of self-assembling peptides with binding affinity to hyaluronan |
title |
Design and synthesis of self-assembling peptides with binding affinity to hyaluronan |
spellingShingle |
Design and synthesis of self-assembling peptides with binding affinity to hyaluronan Dória, Rita Saraiva de Aragão da Silva Domínio/Área Científica::Ciências Médicas::Biotecnologia Médica |
title_short |
Design and synthesis of self-assembling peptides with binding affinity to hyaluronan |
title_full |
Design and synthesis of self-assembling peptides with binding affinity to hyaluronan |
title_fullStr |
Design and synthesis of self-assembling peptides with binding affinity to hyaluronan |
title_full_unstemmed |
Design and synthesis of self-assembling peptides with binding affinity to hyaluronan |
title_sort |
Design and synthesis of self-assembling peptides with binding affinity to hyaluronan |
author |
Dória, Rita Saraiva de Aragão da Silva |
author_facet |
Dória, Rita Saraiva de Aragão da Silva |
author_role |
author |
dc.contributor.none.fl_str_mv |
Azevedo, Helena Collis, Dominic Veritati - Repositório Institucional da Universidade Católica Portuguesa |
dc.contributor.author.fl_str_mv |
Dória, Rita Saraiva de Aragão da Silva |
dc.subject.por.fl_str_mv |
Domínio/Área Científica::Ciências Médicas::Biotecnologia Médica |
topic |
Domínio/Área Científica::Ciências Médicas::Biotecnologia Médica |
description |
Hyaluronan (HA) is a natural polymer that due to its viscoelasticity, good biocompatibility and a conformational flexibility, has been a polysaccharide of great interest to the scientists that is used in various biomedical and clinical applications such as tissue engineering, biomaterials engineering and cosmetics. This project aimed to explore the self-assembly between hyaluronan (HA) and HA-binding peptides derived from Pep-1[NH2-GAHWQFNALTVR-NH2], a peptide known to bind HA and identified by phage display. Six variations of Pep-1 were synthesized to test if they can form new nanostructures with HA. Peptides with alkyl chains allow the formation of highly stable self-assembled nanostructures. Considering this fact, were synthesized four peptides with these properties in order to try the interaction between them and hyaluronan. On the other hand, thiols (compounds that contain a SH group) can bond to gold due to the capability to be chemisorbed on metal surfaces, forming a very stable metal-sulfur bonds. Therefore, it was synthesized a peptide with a tail constituted by Mercaptoethanol acid that is expected to react with gold, displaying the Pep-1 free to interact with HA. Electrospray Ionization Mass Spectrometry and High-Performance Liquid Chromatography techniques were used to characterize and purify the peptides, respectively. After the experimental work and its results, it was concluded that by increasing the percentage of Pep-1 is possible to see an interaction between it and hyaluronan. Peptides with longer alkyl chain are to hydrophobic to be purified and consequently it was impossible to study the interaction between them and HA.When the alkyl chains become shorter, the peptides become less hydrophobic and their purification is possible. Though, the peptides with shorter chains can´t allow the formation of self-assembled structures. The peptide that has a Mercaptoethanol acid is hydrophobic but, its purification is possible. More tests should be done in order to study and analyze if the interaction between this last peptide and HA is possible. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-07-06 2017-01 2017-07-06T00:00:00Z 2022-03-15T16:19:29Z |
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.uri.fl_str_mv |
http://hdl.handle.net/10400.14/37036 TID:202729842 |
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http://hdl.handle.net/10400.14/37036 |
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eng |
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eng |
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info:eu-repo/semantics/openAccess |
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openAccess |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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