Insights on the mechanism of formation of protein microspheres in a biphasic system

Detalhes bibliográficos
Autor(a) principal: Silva, Raquel
Data de Publicação: 2012
Outros Autores: Ferreira, Helena, Azóia, Nuno G., Shimanovich, Ulyana, Freddi, G., Gedanken, Aharon, Paulo, Artur Cavaco
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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spelling 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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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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