Solid-phase peptide synthesis in highly loaded conditions

Página do item simplificado
dc.contributor.authorNakaie, Clovis R. [UNIFESP]
dc.contributor.authorOliveira, Eliandre
dc.contributor.authorVicente, Eduardo F.
dc.contributor.authorJubilut, Guita N. [UNIFESP]
dc.contributor.authorSouza, Sinval E. G. [UNIFESP]
dc.contributor.authorMarchetto, Reinaldo
dc.contributor.authorCilli, Eduardo M.
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionBarcelona Sci Pk
dc.contributor.institutionUNESP Univ Estadual Paulista
dc.date.accessioned2016-01-24T14:06:08Z
dc.date.available2016-01-24T14:06:08Z
dc.date.issued2011-02-01
dc.description.abstractThe use of very highly substituted resins has been avoided for peptide synthesis due to the aggravation of chain-chain interactions within beads. To better evaluate this problem, a combined solvation-peptide synthesis approach was herein developed taking as models, several peptide-resins and with peptide contents values increasing up to near 85%. Influence of peptide sequence and loading to solvation characteristics of these compounds was observed. Moreover, chain-chain distance and chain concentration within the bead were also calculated in different loaded conditions. of note, a severe shrinking of beads occurred during the alpha-amine deprotonation step only when in heavily loaded resins, thus suggesting the need for the modification of the solvent system at this step. Finally, the yields of different syntheses in low and heavily loaded conditions were comparable, thus indicating the feasibility of applying this latter prohibitive chemical synthesis protocol. We thought these results might be basically credited to the possibility, without the need of increasing molar excess of reactants, of carrying out the coupling reaction in higher concentration of reactants - near three to seven folds - favored by the use of smaller amount of resin. Additionally, the alteration in the solvent system at the alpha-amine deprotonation step might be also improving the peptide synthesis when in heavily loaded experimental protocol. (C) 2011 Elsevier Inc. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo UNIFESP, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationBarcelona Sci Pk, Prote Platform, E-08028 Barcelona, Spain
dc.description.affiliationUNESP Univ Estadual Paulista, Inst Quim, Dept Bioquim & Tecnol Quim, Araraquara, SP, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo UNIFESP, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipFADA
dc.format.extent101-109
dc.identifierhttp://dx.doi.org/10.1016/j.bioorg.2011.01.001
dc.identifier.citationBioorganic Chemistry. San Diego: Academic Press Inc Elsevier Science, v. 39, n. 1-3, p. 101-109, 2011.
dc.identifier.doi10.1016/j.bioorg.2011.01.001
dc.identifier.issn0045-2068
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/33412
dc.identifier.wosWOS:000307423100013
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBioorganic Chemistry
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectPeptideen
dc.subjectPeptide synthesisen
dc.subjectPeptide-resin solvationen
dc.subjectPolymeren
dc.subjectPolarityen
dc.titleSolid-phase peptide synthesis in highly loaded conditionsen
dc.typeinfo:eu-repo/semantics/article
Arquivos
Coleções
EPM - Artigos