Abstract |
Evidence that the galectin family of proteins plays crucial roles in cancer, inflammation, and immunity has accumulated over the last decade. The galectins have consequently emerged as interesting drug targets. A majority of galectin functions occurs by means of cross-linking glycoproteins and by doing so controlling glycoprotein cellular localization and residence times. The glycoprotein cross-linking occurs when galectin dimers or multimers, or galectins with two binding sites, bind galactose-containing glycans of the glycoproteins. Such galectin- glycan interactions have been successfully blocked with compounds having multivalent presentation of galactose, lactose, or N-acetyllactosamine, with peptides, and with small carbohydrate ( galactose) derivatives. This review summarizes and analyzes attempts to develop efficient and selective small-molecule galectin inhibitors through derivatization of monosaccharides, mainly galactosides, with non- carbohydrate structures that protrude into subsites adjacent to the core-conserved galactose-recognizing site of the galectins.
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Authors | Christopher T Oberg, Hakon Leffler, Ulf J Nilsson |
Journal | Chimia
(Chimia (Aarau))
Vol. 65
Issue 1-2
Pg. 18-23
( 2011)
ISSN: 0009-4293 [Print] Switzerland |
PMID | 21469439
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
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Chemical References |
- Galactosides
- Galectins
- Monosaccharides
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Topics |
- Drug Design
- Galactosides
(chemical synthesis, chemistry, pharmacology)
- Galectins
(antagonists & inhibitors)
- Molecular Weight
- Monosaccharides
(chemical synthesis, chemistry, pharmacology)
- Structure-Activity Relationship
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