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, E. M.
dc.contributor.institutionUNESP
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.accessioned2016-01-24T12:38:01Z
dc.date.available2016-01-24T12:38:01Z
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.affiliationUnifespUNIFESP, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
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.urihttp://repositorio.unifesp.br/handle/11600/28442
dc.identifier.wosWOS:000231830700005
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofJournal of Peptide Science
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.subjectNMRen
dc.subjecthigh-resolution magic angle spinningen
dc.subjectsolid-phase synthesisen
dc.subjectresinen
dc.subjectpeptideen
dc.titleStudy of the effect of the peptide loading and solvent system in SPPS by HRMAS-NMRen
dc.typeinfo:eu-repo/semantics/article
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