Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9749063 | Journal of Chromatography A | 2005 | 8 Pages |
Abstract
A combination of rational design based on mimicking natural protein-carbohydrate interactions and solid-phase combinatorial chemistry has led to the identification of an affinity ligand which displays selectivity for the mannose moiety of glycoproteins. The ligand was initially identified as 32/18, a triazine scaffold substituted with 2-acetylpyrrole (32) and 5-aminoindan (18). However, characterisation of the immobilised ligand by release from the matrix via a cleavable linker, (4s,5s)-4,5-di(aminomethyl)-2,2-dimethyldioxolane, and using a non-destructive on-resin method, 13C NMR spectroscopy, confirmed that the putative ligand 32/18 was, in fact, 18/18, the disubstituted 5-aminoindan. 1H NMR studies on the interaction of â-d-methylmannoside with the ligand 18/18 in solution confirm the involvement of the hydroxyl group in the C-2 position.
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Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Uma D. Palanisamy, Christopher R. Lowe,