Insights on the mechanism of formation of protein microspheres in a biphasic system
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/22652 |
Resumo: | Microspheres of bovine serum albumin (BSA) and silk fibroin are produced by applying ultrasound in a biphasic system consisting of an aqueous protein solution and an organic solvent. The protein microspheres are dispersed in an aqueous media where the protein remains at the interface covering the organic solvent. This only occurs when high shear forces are applied that induce changes to force the protein to the interface. Fourier transform infrared results indicate a large increase in the content of the β-sheet during the formation of silk fibroin microspheres. Molecular dynamics simulations show a clear adaption on the 3D structure of BSA when stabilized at the interface, without major changes in secondary structure. Further studies demonstrate that high water content, oil solvents, and larger peptides with separated and clear hydrophobic and hydrophilic areas lead to more stable and smaller spheres. This is the first time that these results are presented. We also present herein the rationale to produce tailored protein microspheres with a controlled size, controlled charge, and increased stability. |
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Insights on the mechanism of formation of protein microspheres in a biphasic systemAmino acidsHydrophobic/hydrophilic balanceMicrospheresProteinsSonochemistryScience & TechnologyMicrospheres of bovine serum albumin (BSA) and silk fibroin are produced by applying ultrasound in a biphasic system consisting of an aqueous protein solution and an organic solvent. The protein microspheres are dispersed in an aqueous media where the protein remains at the interface covering the organic solvent. This only occurs when high shear forces are applied that induce changes to force the protein to the interface. Fourier transform infrared results indicate a large increase in the content of the β-sheet during the formation of silk fibroin microspheres. Molecular dynamics simulations show a clear adaption on the 3D structure of BSA when stabilized at the interface, without major changes in secondary structure. Further studies demonstrate that high water content, oil solvents, and larger peptides with separated and clear hydrophobic and hydrophilic areas lead to more stable and smaller spheres. This is the first time that these results are presented. We also present herein the rationale to produce tailored protein microspheres with a controlled size, controlled charge, and increased stability.This work was supported by Lidwine Project-Multifunctional medical textiles for wound (e.g., Decubitus) prevention and improved wound healing NMP2-CT-2006-026741. H.F. thanks POPH/FSE for cofinancing and FCT for Fellowship SFRH/BPD/38939/2007. We acknowledge Silvia Cappellozza from "Sezione Specializzata per la Bachicoltura" for the supply of silk cocoons.ACS PublicationsUniversidade do MinhoSilva, RaquelFerreira, HelenaAzóia, Nuno G.Shimanovich, UlyanaFreddi, G.Gedanken, AharonPaulo, Artur Cavaco20122012-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/22652eng1543-838410.1021/mp300182723025530http://dx.doi.org/10.1021/mp3001827info: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:RCAAP2023-07-21T12:12:20Zoai:repositorium.sdum.uminho.pt:1822/22652Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:04:14.677687Repositório 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 |
Insights on the mechanism of formation of protein microspheres in a biphasic system |
title |
Insights on the mechanism of formation of protein microspheres in a biphasic system |
spellingShingle |
Insights on the mechanism of formation of protein microspheres in a biphasic system Silva, Raquel Amino acids Hydrophobic/hydrophilic balance Microspheres Proteins Sonochemistry Science & Technology |
title_short |
Insights on the mechanism of formation of protein microspheres in a biphasic system |
title_full |
Insights on the mechanism of formation of protein microspheres in a biphasic system |
title_fullStr |
Insights on the mechanism of formation of protein microspheres in a biphasic system |
title_full_unstemmed |
Insights on the mechanism of formation of protein microspheres in a biphasic system |
title_sort |
Insights on the mechanism of formation of protein microspheres in a biphasic system |
author |
Silva, Raquel |
author_facet |
Silva, Raquel Ferreira, Helena Azóia, Nuno G. Shimanovich, Ulyana Freddi, G. Gedanken, Aharon Paulo, Artur Cavaco |
author_role |
author |
author2 |
Ferreira, Helena Azóia, Nuno G. Shimanovich, Ulyana Freddi, G. Gedanken, Aharon Paulo, Artur Cavaco |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Silva, Raquel Ferreira, Helena Azóia, Nuno G. Shimanovich, Ulyana Freddi, G. Gedanken, Aharon Paulo, Artur Cavaco |
dc.subject.por.fl_str_mv |
Amino acids Hydrophobic/hydrophilic balance Microspheres Proteins Sonochemistry Science & Technology |
topic |
Amino acids Hydrophobic/hydrophilic balance Microspheres Proteins Sonochemistry Science & Technology |
description |
Microspheres of bovine serum albumin (BSA) and silk fibroin are produced by applying ultrasound in a biphasic system consisting of an aqueous protein solution and an organic solvent. The protein microspheres are dispersed in an aqueous media where the protein remains at the interface covering the organic solvent. This only occurs when high shear forces are applied that induce changes to force the protein to the interface. Fourier transform infrared results indicate a large increase in the content of the β-sheet during the formation of silk fibroin microspheres. Molecular dynamics simulations show a clear adaption on the 3D structure of BSA when stabilized at the interface, without major changes in secondary structure. Further studies demonstrate that high water content, oil solvents, and larger peptides with separated and clear hydrophobic and hydrophilic areas lead to more stable and smaller spheres. This is the first time that these results are presented. We also present herein the rationale to produce tailored protein microspheres with a controlled size, controlled charge, and increased stability. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012 2012-01-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/1822/22652 |
url |
http://hdl.handle.net/1822/22652 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1543-8384 10.1021/mp3001827 23025530 http://dx.doi.org/10.1021/mp3001827 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
ACS Publications |
publisher.none.fl_str_mv |
ACS Publications |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
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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1799132451366240256 |