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Inhibition of Galectins with Small Molecules

Öberg, Christopher LU ; Leffler, Hakon LU and Nilsson, Ulf LU (2011) In Chimia 65(1-2). p.18-23
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 gly-coproteirl 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... (More)
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 gly-coproteirl 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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Cancer, Galectin, Immunity, Inflammation, Inhibitor
in
Chimia
volume
65
issue
1-2
pages
18 - 23
publisher
Swiss Chemical Society
external identifiers
  • wos:000287981400004
  • pmid:21469439
  • scopus:79952576615
ISSN
0009-4293
DOI
10.2533/chimia.2011.18
language
English
LU publication?
yes
id
bcc019e3-c3e2-43a3-96c3-796a55b73c8f (old id 1868550)
date added to LUP
2011-04-19 12:09:54
date last changed
2017-09-17 06:44:05
@article{bcc019e3-c3e2-43a3-96c3-796a55b73c8f,
  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 gly-coproteirl 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.},
  author       = {Öberg, Christopher and Leffler, Hakon and Nilsson, Ulf},
  issn         = {0009-4293},
  keyword      = {Cancer,Galectin,Immunity,Inflammation,Inhibitor},
  language     = {eng},
  number       = {1-2},
  pages        = {18--23},
  publisher    = {Swiss Chemical Society},
  series       = {Chimia},
  title        = {Inhibition of Galectins with Small Molecules},
  url          = {http://dx.doi.org/10.2533/chimia.2011.18},
  volume       = {65},
  year         = {2011},
}