Diphtheria toxoid conformation in the context of its nanoencapsulation within liposomal particles sandwiched by chitosan

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dc.contributor.author Rescia, Vanessa C. [UNIFESP]
dc.contributor.author Ramos, Henrique R.
dc.contributor.author Takata, Celia S.
dc.contributor.author Araujo, Pedro S. de
dc.contributor.author Costa, Maria H. B. da
dc.date.accessioned 2016-01-24T14:16:52Z
dc.date.available 2016-01-24T14:16:52Z
dc.date.issued 2011-06-01
dc.identifier http://dx.doi.org/10.3109/08982104.2010.491072
dc.identifier.citation Journal of Liposome Research. London: Informa Healthcare, v. 21, n. 2, p. 116-123, 2011.
dc.identifier.issn 0898-2104
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/33790
dc.description.abstract Chitosan (alpha alpha-(1-4)-amino-2-deoxy-beta beta-D-glucan) is a deacetylated form of chitin, a polysaccharide from crustacean shells. Its unique characteristics, such as positive charge, biodegradability, biocompatibility, nontoxicity, and rigid structure, make this macromolecule ideal for an oral vaccine delivery system. We prepared reverse-phase evaporation vesicles (REVs) sandwiched by chitosan (Chi) and polyvinylic alcohol (PVA). However, in this method, there are still some problems to be circumvented related to protein stabilization. During the inverted micelle phase of protein nanoencapsulation, hydrophobic interfaces are expanded, leading to interfacial adsorption, followed by protein unfolding and aggregation. Here, spectroscopic and immunological techniques were used to ascertain the effects of the Hoffmeister series ions on diphtheria toxoid (Dtxd) stability during the inverted micelle phase. A correlation was established between the salts used in aqueous solutions and the changes in Dtxd solubility and conformation. Dtxd alpha alpha-helical content was quite stable, which led us to conclude that encapsulation occurred without protein aggregation or without exposition of hydrophobic residues. Dtxd aggregation was 98% avoided by the kosmotropic, PO<SU2--</SU(4). This ion was used to prepare a stable Dtxd and immunologically recognized REV-Chi-PVA formulation in the presence of 50 mM of PO<SU2--</SU(4). Under these conditions, the Dtxd retained its immunological identity. Therefore, we could obtain the maximum Dtxd solubility and stability after contact with CH(3)CO(2)C(2)H(5) to begin its nanoencapsulation within ideal conditions. This was a technological breakthrough, because a simple solution, such as salt, addition avoided heterologous protein use.</. en
dc.description.sponsorship Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorship Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorship Fundacao Butantan
dc.description.sponsorship Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.format.extent 116-123
dc.language.iso eng
dc.publisher Informa Healthcare
dc.relation.ispartof Journal of Liposome Research
dc.rights Acesso restrito
dc.subject Liposome-vaccine delivery en
dc.subject Hoffmeister serie ions en
dc.subject protein stabilization en
dc.subject interaction protein/organic solvent en
dc.subject protein nanoencapsulation en
dc.title Diphtheria toxoid conformation in the context of its nanoencapsulation within liposomal particles sandwiched by chitosan en
dc.type Artigo
dc.rights.license http://informahealthcare.com/userimages/ContentEditor/1255620309227/Copyright_And_Permissions.pdf
dc.contributor.institution Ctr Biotecnol
dc.contributor.institution Div Desenvolvimento Tecnol & Prod
dc.contributor.institution Universidade de São Paulo (USP)
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Ctr Biotecnol, Lab Microesferas & Lipossomas, BR-05503900 São Paulo, Brazil
dc.description.affiliation Ctr Biotecnol, Lab Biotecnol Mol, BR-05503900 São Paulo, Brazil
dc.description.affiliation Div Desenvolvimento Tecnol & Prod, São Paulo, Brazil
dc.description.affiliation Univ São Paulo, Inst Quim, Dept Bioquim, BR-01498 São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Med, Disciplina Clin Med, São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Med, Disciplina Clin Med, São Paulo, Brazil
dc.description.sponsorshipID FAPESP: 00/10970-7
dc.description.sponsorshipID CNPq: 302047/2008-5
dc.description.sponsorshipID CNPq: 454177/2009-7
dc.identifier.doi 10.3109/08982104.2010.491072
dc.description.source Web of Science
dc.identifier.wos WOS:000290734600003



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