Monitoring the chemical assembly of a transmembrane bradykinin receptor fragment: Correlation between resin solvation, peptide chain mobility, and rate of coupling

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dc.contributor.author Oliveira, E.
dc.contributor.author Cilli, Eduardo Maffud [UNIFESP]
dc.contributor.author Miranda, A.
dc.contributor.author Jubilut, Guita Nicolaewsky [UNIFESP]
dc.contributor.author Albericio, F.
dc.contributor.author Andreu, D.
dc.contributor.author Paiva, Antonio Cechelli de Mattos [UNIFESP]
dc.contributor.author Schreier, Shirley [UNIFESP]
dc.contributor.author Tominaga, Mineko [UNIFESP]
dc.contributor.author Nakaie, Clovis Ryuichi [UNIFESP]
dc.date.accessioned 2018-06-15T17:22:29Z
dc.date.available 2018-06-15T17:22:29Z
dc.date.issued 2002-11-01
dc.identifier https://doi.org/10.1002/1099-0690(200211)2002:21<3686
dc.identifier.citation European Journal Of Organic Chemistry. Weinheim: Wiley-v C H Verlag Gmbh, n. 21, p. 3686-3694, 2002.
dc.identifier.issn 1434-193X
dc.identifier.uri http://repositorio.unifesp.br/11600/43621
dc.description.abstract A combined resin solvation-peptide chain motion and kinetics of coupling reaction approach was applied to monitor details of the synthesis of TM-34, a 34-residue transmembrane segment of the bradykinin receptor. The dynamics of resin-bound peptide fragments attached to a stable free radical amino acid were examined by EPR spectroscopy. In agreement with an abrupt decrease (from 83 to 43%) in peptide purity occurring in the 12-16 region when DMF was used, a much more strongly immobilized chain population was detected, especially at the 12-mer stage. Conversely, faster couplings and improved synthesis were observed in 20% DMSO/NMP, probably due to the higher chain mobility in this mixed solvent. In addition, findings relating to solvation of peptide resins seemed to corroborate the previously advanced proposition that the 1:1 sum of electron acceptor and electron donor properties of a solvent can be considered to be an alternative and more appropriate parameter for its polarity. en
dc.format.extent 3686-3694
dc.language.iso eng
dc.publisher Wiley-Blackwell
dc.relation.ispartof European Journal Of Organic Chemistry
dc.rights Acesso restrito
dc.subject bradykinin en
dc.subject EPR spectroscopy en
dc.subject membranes en
dc.subject peptides en
dc.subject resins en
dc.title Monitoring the chemical assembly of a transmembrane bradykinin receptor fragment: Correlation between resin solvation, peptide chain mobility, and rate of coupling en
dc.type Resenha
dc.rights.license http://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution Univ Barcelona
dc.contributor.institution Universidade de São Paulo (USP)
dc.description.affiliation Univ Fed Sao Paulo, Dept Biophys, BR-04044020 Sao Paulo, Brazil
dc.description.affiliation Univ Barcelona, Dept Organ Chem, E-08028 Barcelona, Spain
dc.description.affiliation Univ Sao Paulo, Dept Biochem, Inst Chem, BR-05513970 Sao Paulo, Brazil
dc.description.affiliationUnifesp Univ Fed Sao Paulo, Dept Biophys, BR-04044020 Sao Paulo, Brazil
dc.identifier.doi 10.1002/1099-0690(200211)2002:21<3686
dc.description.source Web of Science
dc.identifier.wos WOS:000179197900022



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