کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1390506 | 983093 | 2011 | 8 صفحه PDF | دانلود رایگان |
To enable enzymatic coupling of saccharides to proteins, several di- and trisaccharides were hydroxy-arylated using anhydrous transesterification with methyl 3-(4-hydroxyphenyl)propionate, catalyzed by potassium carbonate. This transesterification resulted in the attachment of up to 3 hydroxy-aryl units per oligosaccharide molecule, with the monosubstituted product being by far the most abundant. The alkaline reaction conditions, however, resulted in a partial breakdown of reducing sugars. This breakdown could easily be bypassed by a preceding sugar reduction step converting them to polyols. Hydroxy-arylated products were purified by using solid phase extraction, based on the number of hydroxy-aryl moieties attached. Monohydroxy-arylated saccharose was subsequently linked to a tyrosine-containing tripeptide using horseradish peroxidase, as monitored by LC–MSn. This proof of principle for peptide and protein glycation with a range of possible saccharides and glycosidic polyols can lead to products with unique new properties.
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► Oligosaccharides and glycosidic polyols are hydroxy-arylated by transesterification.
► Hydroxy-arylated oligosaccharides are fractionated using solid phase extraction.
► Hydroxy-arylated saccharose is coupled to Gly-Tyr-Gly using horseradish peroxidase.
► Proof of principle given for protein glycation via an introduced phenolic linker.
Journal: Carbohydrate Research - Volume 346, Issue 8, 1 June 2011, Pages 1005–1012