Correlation between the mobility of spin-labeled peptide chains and resin solvation: An approach to optimize the synthesis of aggregating sequences

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorCilli, Eduardo Maffud
dc.creatorMarchetto, Reinaldo
dc.creatorSchreier, S.
dc.creatorNakaie, C. R.
dc.date2014-05-20T15:22:07Z
dc.date2016-10-25T17:55:47Z
dc.date2014-05-20T15:22:07Z
dc.date2016-10-25T17:55:47Z
dc.date1999-12-10
dc.date.accessioned2017-04-05T23:35:11Z
dc.date.available2017-04-05T23:35:11Z
dc.identifierJournal of Organic Chemistry. Washington: Amer Chemical Soc, v. 64, n. 25, p. 9118-9123, 1999.
dc.identifier0022-3263
dc.identifierhttp://hdl.handle.net/11449/33180
dc.identifierhttp://acervodigital.unesp.br/handle/11449/33180
dc.identifier10.1021/jo991035o
dc.identifierWOS:000084270600021
dc.identifier0000-0002-4767-0904
dc.identifierhttp://dx.doi.org/10.1021/jo991035o
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/877355
dc.descriptionResin solvation properties affect the efficiency of the coupling reactions in solid-phase peptide synthesis. Here we report a novel approach to evaluate resin solvation properties, making use of spin label electron paramagnetic resonance (EPR) spectroscopy. The aggregating VVLGAAIV and ING sequences were assembled in benzhydrylamine-resin with different amino group contents (up to 2.6 mmol/g) to examine the extent of chain association within the beads. These model peptidyl-resins were first labeled at their N-terminus with the amino acid spin label 2,2,6,6-tetramethylpiperidine-N-oxyl-4-amino-4-carboxylic acid (Toac). Their solvation properties in different solvents were estimated, either by bead swelling measurement or by assessing the dynamics of their polymeric matrixes through the analysis of Toac EPR spectra, and were correlated with the yield of the acylation reaction. In most cases the coupling rate was found to depend on bead swelling. Comparatively, the EPR approach was more effective. Line shape analysis allowed the detection of more than one peptide chain population, which influenced the reaction. The results demonstrated the unique potential of EPR spectroscopy not only for improving the yield of peptide synthesis, even in challenging conditions, but also for other relevant polymer-supported methodologies in chemistry and biology.
dc.languageeng
dc.publisherAmer Chemical Soc
dc.relationJournal of Organic Chemistry
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.titleCorrelation between the mobility of spin-labeled peptide chains and resin solvation: An approach to optimize the synthesis of aggregating sequences
dc.typeOtro


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