Esterification of 9-Fluorenylmethoxycarbonyl-glycosylated serine and cysteine derivatives with an hydroxymethyl resin
| Autor: | Danièle Cantacuzene, Estelle Harth‐Fritschy |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Glycosylation
Magnetic Resonance Spectroscopy Tetrafluoroborate Alcohol Biochemistry Medicinal chemistry Serine chemistry.chemical_compound Endocrinology Organic chemistry Hydroxymethyl Amino Acid Sequence Cysteine Amino Acids Racemization Chromatography High Pressure Liquid chemistry.chemical_classification Fluorenes Alanine Esterification Triazines Stereoisomerism Amino acid Dinitrobenzenes chemistry Reagent Indicators and Reagents Peptides Resins Plant |
| Zdroj: | The Journal of Peptide Research. 50:415-420 |
| ISSN: | 1397-002X |
| Popis: | Esterification of glycosylated serine and cysteine derivatives with a 4-alkoxybenzyl alcohol (Wang) resin is described. The classical methods of ester bond formation (symmetrical anhydride, 2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium tetrafluoroborate [TBTU]. /4-dimethylaminopyridine [DMAP]. with or without 1-hydroxybenzotriazole [HOBT]., pentafluorophenyl [Pfp]. esters) gave high percentages of racemization of the glycosylated serine or cysteine residues. To reduce the d-amino acid content, we found that the best results were obtained with the highly efficient MSNT reagent (2,4,6-mesitylenesulfonyl-3-nitro-1,2,4-triazolide), which gave a high yield of substitution of the resin and the lowest percentage of racemization. A difference in behavior was observed between the two amino acids. The glycosylated cysteine derivative always gave lower racemization than the analogous glycosylated serine. |
| Databáze: | OpenAIRE |
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