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2 at room temperature.
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70350514338
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This compound was kindly provided as trifluoroacetic salt by UFPeptides s.r.L. (University of Ferrara)
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This compound was kindly provided as trifluoroacetic salt by UFPeptides s.r.L. (University of Ferrara).
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59
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70350488746
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note
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Surprisingly, the use of lower amounts of DPAP (50 and 10mol%) were not sufficient for achieving a complete glycosylation of this peptide.
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Max = 254nm, 70W) solutions of BSA and sugar la in DMSO-phosphate buffer (pH 7.4) for 3-6 h either in the absence or presence of 4,4'-azobis(4cyanovaleric acid) as the sensitizer.
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Unfortunately, pre-treatment of glycosylated BSA 10 with dithiothreitol (DTT) for protein disulfide bonds reduction followed by excess iodoacetamide (IAA) sulfhydryl groups derivatization produced tryptic fragments, which displayed the acetamido group at cysteine residues 34, 75, and, very likely, at Cys-91 in place of the expected galactoside moiety (see the Supporting Information). This outcome is tentatively explained by the formation of intermediate S-acetamido sulfonium derivatives of glycosylated cysteine peptide fragments followed by a β-elimination process, which should result in the formation of the allyl galactoside la and S-acetamido peptide fragments (see Scheme S1). The occurrence of this undesired side reaction that makes the DTT/IAA analysis method unsuitable for the characterization of glycosylated BSA 10 was also demonstrated by using the less complex glycopeptide 9 as the substrate (Supporting Information). For a deeper discussion on the β-elimination reaction of dialkylated sulfonium derivatives of Cys and the synthetic potential of related oxidative elimination of Cys for protein modification, see ref. [8].
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