Inhibition of Galectins with Small Molecules

CHIMIA

卷:65

Ulf J. Nilsson¹  Christopher T. Öberg¹  Hakon Leffler² 

[1] Organic Chemistry, Lund University POB 124, SE-221 00 Lund, Sweden;

[2] Section MIG, Department of Laboratory Medicine Lund University Sölvegatan 23, SE-223 62 Lund, Sweden;

关键词: Cancer;    Galectin;    Immunity;    Inflammation;    Inhibitor;   

DOI  :  10.2533/chimia.2011.18

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown