You are in the accessibility menu

Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorValente, A. P.-
dc.contributor.authorAlmeida, FCL-
dc.contributor.authorNakaie, C. R.-
dc.contributor.authorSchreier, S.-
dc.contributor.authorCrusca, E.-
dc.contributor.authorCilli, Eduardo Maffud-
dc.identifier.citationJournal of Peptide Science. Chichester: John Wiley & Sons Ltd, v. 11, n. 9, p. 556-563, 2005.-
dc.description.abstractThe SPPS methodology has continuously been investigated as a valuable model to monitor the solvation properties of polymeric materials. In this connection, the present work applied HRMAS-NMR spectroscopy to examine the dynamics of an aggregating peptide sequence attached to a resin core with varying peptide loading (up to 80%) and solvent system. Low and high substituted BHAR were used for assembling the VQAAIDYING sequence and some of its minor fragments. The HRMAS-NMR results were in agreement with the swelling of each resin, i.e. there was an improved resolution of resonance peaks in the better solvated conditions. Moreover, the peptide loading and the attached peptide sequence also affected the spectra. Strong peptide chain aggregation was observed mainly in highly peptide loaded resins when solvated in CDCl3. Conversely, due to the better swelling of these highly loaded resins in DMSO, improved NMR spectra were acquired in this polar aprotic solvent, thus enabling the detection of relevant sequence-dependent conformational alterations. The more prominent aggregation was displayed by the VQAAIDYING segment and not by any of its intermediary fragments and these findings were also corroborated by EPR studies of these peptide-resins labelled properly with an amino acid-type spin probe. Copyright (c) 2005 European Peptide Society and John Wiley & Sons, Ltd.en
dc.sourceWeb of Science-
dc.subjecthigh-resolution magic angle spinningpt
dc.subjectsolid-phase synthesispt
dc.titleStudy of the effect of the peptide loading and solvent system in SPPS by HRMAS-NMRen
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)-
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)-
dc.description.affiliationUNESP, Dept Biochem & Chem Technol, BR-14800900 Araraquara, SP, Brazil-
dc.description.affiliationUSP, Inst Chem, Dept Biochem, BR-05599970 São Paulo, Brazil-
dc.description.affiliationUNIFESP, Dept Biophys, BR-04044020 São Paulo, Brazil-
dc.description.affiliationUFRJ, Dept Med Biochem, Ctr Nacl Ressonancia Magnet Nucl Jiri Jonas, Rio de Janeiro, Brazil-
dc.description.affiliationUnespUNESP, Dept Biochem & Chem Technol, BR-14800900 Araraquara, SP, Brazil-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofJournal of Peptide Science-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.