Study of the effect of the peptide loading and solvent system in SPPS by HRMAS-NMR

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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 [UNESP]
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.date.accessioned2014-05-20T15:27:20Z
dc.date.available2014-05-20T15:27:20Z
dc.date.issued2005-09-01
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.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.format.extent556-563
dc.identifierhttp://dx.doi.org/10.1002/psc.659
dc.identifier.citationJournal of Peptide Science. Chichester: John Wiley & Sons Ltd, v. 11, n. 9, p. 556-563, 2005.
dc.identifier.doi10.1002/psc.659
dc.identifier.issn1075-2617
dc.identifier.lattes9424346762460416
dc.identifier.orcid0000-0002-4767-0904
dc.identifier.urihttp://hdl.handle.net/11449/37342
dc.identifier.wosWOS:000231830700005
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofJournal of Peptide Science
dc.relation.ispartofjcr1.969
dc.relation.ispartofsjr0,883
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectNMRpt
dc.subjecthigh-resolution magic angle spinningpt
dc.subjectsolid-phase synthesispt
dc.subjectresinpt
dc.subjectpeptidept
dc.titleStudy of the effect of the peptide loading and solvent system in SPPS by HRMAS-NMRen
dc.typeArtigo
dcterms.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dcterms.rightsHolderWiley-Blackwell
unesp.author.lattes9424346762460416
unesp.author.orcid0000-0002-4767-0904[6]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Química, Araraquarapt

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